| 1. |
- Mamma, D., et al.
(författare)
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Combined photo-assisted and biological treatment of industrial oily wastewater
- 2004
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Ingår i: Journal of Environmental Science and Health. Part A. - 1093-4529 .- 1532-4117. ; 39:3, s. 729-740
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Tidskriftsartikel (refereegranskat)abstract
- In the present study an oily wastewater from the lubricant unit of a petroleum company was evaluated by combining the sequence photo-assisted oxidation-Pseudomonas putida DSM 437. The wastewater contained various alcohols, acids and phenolic compounds. From the above mentioned compounds the biodegradation of ethylene glycol, phenol, o-cresol and p-cresol was examined. The direct biodegradation of the wastewater using P. putida DSM 437 resulted in 95% ethylene glycol assimilation while phenol, o-cresol and p-cresol assimilation was in the range of 27% to 40%. In order to increase the degradation of the phenolic compounds photo-assisted oxidation was applied to the wastewater using UV/H2O2 as a pretreatment step to biological degradation. Fe(III) were used in order to accelerate the formation of the hydroxyl radicals and consequently the overall photo-oxidation process. The addition of Fe(III) ions resulted in 30% decrease of COD within the first 10 min while the respected value without iron ions was 5%. he combined photo-assisted oxidation and biodegradation of the wastewater resulted in 100% removal of ethylene glycol. The overall degradation of phenol was 78% while the 59% and 84% of the initial o-cresol and p-cresol respectively, were removed from the wastewater. The-combined process resulted in 72% of COD removal.
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| 2. |
- Agnantiari, G., et al.
(författare)
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A Purified α-galactosidase from aspergillus niger with enhanced kinetic characteristics
- 1991
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Ingår i: Acta Biotechnologica. - : Wiley. - 0138-4988 .- 1521-3846. ; 11:5, s. 479-484
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Tidskriftsartikel (refereegranskat)abstract
- Extracellular α-galactosidase from Aspergillus niger was purified 128-fold over the crude extract by gel filtration, ion exchange chromatography and chromatofocusing. Certain substrates and end products affected enzyme activity. Among the former p-nitrophenyl-α-galactopyranoside (PNPG) inhibited the enzyme at 1.4 mM while melibiose did not inhibit α-galactosidase at concentrations up to 50 mM. Enzymic end products such as glucose did not inhibit the enzyme at concentrations up to 100 mM while galactose exhibited a competitive inhibition with a Ki = 1.29 mM. The kinetic characteristics of the enzyme compared favourably to other microbial α-galactosidases and make it suitable for food process applications.
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| 3. |
- Bennett, Neil A., et al.
(författare)
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Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Thermomyces lanuginosus ATCC 46882
- 1998
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Ingår i: Carbohydrate Research. - 0008-6215 .- 1873-426X. ; 306:3, s. 445-455
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Tidskriftsartikel (refereegranskat)abstract
- An endoxylanase (1,4-beta-D-xylan xylanohydrolase, EC 3.2.1.8) from the culture filtrates of T. lanuginosus ATCC 46882 was purified to homogeneity by DEAE-Sepharose and Bio-Gel P-30 column chromatographies. The purified endoxylanase had a specific activity of 888.8 mumol min-1 mg-1 protein and accounted for approximately 30% of the total protein secreted by this fungus. The molecular mass of native (non-denatured) and denatured endoxylanase were 26.3 and 25.7 kD as, respectively. Endoxylanase had a pI of 3.7 and was optimally active between pH 6.0-6.5 and at 75 degrees C. The enzyme showed > 50% of its original activity between pH 5.5-9.0 and at 85 degrees C. The pH and temperature stability studies revealed that this endoxylanase was almost completely stable between pH 5.0-9.0 and up to 60 degrees C for 5 h and at pH 10.0 up to 55 degrees C for 5 h. Thin-layer chromatography (TLC) analysis showed that endoxylanase released mainly xylose (Xyl) and xylobiose (Xyl2) from beechwood 4-O-methyl-D-glucuronoxylan, O-acetyl-4-O-methyl-D-glucuronoxylan and rhodymenan (a beta-(1-->3)-beta(1-->4)-xylan). Also, the enzyme released an acidic xylo-oligosaccharide from 4-O-methyl-D-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. The enzyme hydrolysed [1-3H]-xylo-oligosaccharides in an endofashion, but the hydrolysis of [1-3H]-xylotriose appeared to proceed via transglycosylation. since the xylobiose was the predominant product. Endoxylanase was not active on pNPX and pNPC at 40 and 100 mM for up to 6 h, but showed some activity toward pNPX at 100 mM after 20-24 h. The results suggested that the endoxylanase from T. lanuginosus belongs to family 11.
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| 4. |
- Caridis, K A, et al.
(författare)
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Control of catalase production and purity by altering certain nutritional factors of Alternaria alternata growth medium
- 1991
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 13:1, s. 35-38
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Tidskriftsartikel (refereegranskat)abstract
- Both activity level of catalase and presence of glucose oxidase as an impurity were controlled by the type and concentration of nitrogen and carbon source in the culture medium of Alternaria alternata. It was possible to produce glucose oxidase-free catalase at activity levels competing favourably with those reported for other catalase hyperproducing microorganisms.
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| 5. |
- Caridis, Konstantina-Anna, et al.
(författare)
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Simultaneous production of glucose oxidase and catalase by Alternaria alternata
- 1991
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Ingår i: Applied Microbiology and Biotechnology. - 0175-7598 .- 1432-0614. ; 34:6, s. 794-797
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Tidskriftsartikel (refereegranskat)abstract
- A number of factors affecting simultaneous production of cell-bound glucose oxidase and catalase by the fungus Alternaria alternata have been investigated. Consecutive optimization of the type and concentration of nitrogen and carbon source, the initial pH and growth temperature resulted in a simultaneous increase in glucose oxidase and catalase by 780% and 68% respectively. Two second-order equations, describing the combined effect of pH and temperature on the activity of each enzyme, revealed that glucose oxidase had its optima at pH 7.9 and 32.3°C and catalase at pH 8.5 and 18.1°C. Under certain growth conditions, yields as high as 23.5 and 18,100 units/g carbon source for glucose oxidase and catalase, respectively, were simultaneously obtained.
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| 6. |
- Cheilas, T, et al.
(författare)
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Hemicellulolytic activity of Fusarium oxysporum grown on sugar beet pulp. Production of extracellular arabinanase
- 2000
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Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 35:6, s. 557-561
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Tidskriftsartikel (refereegranskat)abstract
- Fusarium oxysporum F3 exhibited hemicellulolytic enzymic activity when grown on sugar beet pulp, a by-product of the sugar industry. The growth medium was specifically optimised for enhanced production of extracellular arabinanase. The optimum medium contained sugar beet pulp (4%, w/v) and corn steep liquor (6%, v/v) as carbon and nitrogen sources, respectively. Arabinanase activity as high as 0.25 U/ml of culture was obtained, which compared favourably to those reported for other microorganisms. Optimal arabinanase activity was observed at pH 6-7 and 50 °C. Investigation of the degradation of the main components of sugar beet pulp showed that arabinose containing polysaccharides and pectin were first degraded, followed by the glucose-containing polysaccharides.
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| 7. |
- Christakopoulos, Paul, et al.
(författare)
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Antimicrobial activity of acidic xylo-oligosaccharides produced by family 10 and 11 endoxylanases
- 2003
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Ingår i: International Journal of Biological Macromolecules. - 0141-8130 .- 1879-0003. ; 31:4-5, s. 171-175
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Tidskriftsartikel (refereegranskat)abstract
- Acidic oligosaccharides were obtained from birchwood xylan by treatment with a Thermoascus aurantiacus family 10 and a Sporotrichum thermophile family 11 endoxylanases. The main difference between the products liberated by xylanases of family 10 and 11 concerned the length of the products containing 4-O-methyl-d-glucuronic acid. The xylanase from T. aurantiacus liberate from glucuronoxylan an aldotetrauronic acid as the shortest acidic fragment in contrast with the enzyme from S. thermophile, which liberated an aldopentauronic acid. Acidic xylooligosaccharides were separated from the hydrolysate by anion-exchange and size-exclusion chromatography (SEC) and the primary structure was determined by 13C NMR spectroscopy. The acidic xylo-oligosaccharides were tested against three Gram-positive and three Gram-negative aerobically grown bacteria, as well as against Helicobacterpylori. Aldopentauronic acid was proved more active against the Gram-positive bacteria and against H. pylori.
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| 8. |
- Christakopoulos, Paul, et al.
(författare)
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Controlling simultaneous production of endoglucanase and beta-glucosidase by Fusarium oxysporum in submerged culture
- 1995
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 17:8, s. 883-888
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Tidskriftsartikel (refereegranskat)abstract
- The simultaneous production of endoglucanase and β-glucosidase by Fusarium oxysporum was investigated in submerged culture. Consecutive optimization of growth conditions resulted in the correction of large activity differences, observed during production of enzymes, and substantially enhanced low enzyme yields. At optimum growth conditions yields as high as 1650 and 232 U per g of carbon source of endoglucanase and β-glucosidase were obtained respectively competing favourably with those reported for microorganisms grown on the same carbon source. The most important kinetic characteristics of the enzymes were the high temperature optima of endoglucanase (60°C) and β-glucosidase (65°C) and the exceptionally high thermostability of endoglucanase. The latter enzyme retained 50% of the activity at pH 5.0 after approximately 6.5 h at 70°C
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| 9. |
- Christakopoulos, Paul, et al.
(författare)
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Direct conversion of sorghum carbohydrates to ethanol by a mixed microbial culture
- 1993
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Ingår i: Bioresource Technology. - 0960-8524 .- 1873-2976. ; 45:2, s. 89-92
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Tidskriftsartikel (refereegranskat)abstract
- The carbohydrates of sweet sorghum were directly converted to ethanol by a mixed culture of Fusarium oxysporum F3 and Saccharomyces cerevisiae 2541. A number of factors affecting this bioconversion was studied. Optimum ethanol yields of 33·2 g/100 g of total sorghum carbohydrates, corresponding to 10·3 g/100 g of fresh stalks, were obtained. These values represented 68·6% of the theoretical yield based on total polysaccharides and exceeded that based on oligosaccharides of sorghum by 53·7%. The results demonstrated that more than half of the sorghum polysaccharides were directly fermented to ethanol, thus making the process worthy of further investigation.
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| 10. |
- Christakopoulos, Paul, et al.
(författare)
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Direct conversion of straw to ethanol by Fusarium oxysporum : Effect of cellulose crystallinity
- 1991
-
Ingår i: Enzyme and microbial technology. - 0141-0229 .- 1879-0909. ; 13:3, s. 272-274
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Tidskriftsartikel (refereegranskat)abstract
- Wheat straw was successfully fermented to ethanol by Fusarium oxysporum F3 in a one-step process. Cellulose crystallinity was found to be a major factor in the bioconversion process. Ethanol yields increased linearly with decreasing crystallinity index. Approximately 80% of straw carbohydrates were converted directly to ethanol with a yield of 0.28 g ethanol/g−1 of straw when the crystallinity index was reduced to 23.6%.
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| 11. |
- Christakopoulos, Paul, et al.
(författare)
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Direct ethanol conversion of pretreated straw by Fusarium oxysporum
- 1991
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Ingår i: Bioresource Technology. - : Elsevier BV. - 0960-8524 .- 1873-2976. ; 35:3, s. 297-300
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Tidskriftsartikel (refereegranskat)abstract
- Factors affecting the direct conversion of alkali pretreated straw to ethanol by Fusarium oxysporum F3 were investigated and the alkali level used for pretreatment and the degree of delignification of straw were found to be the most important. A linear correlation between ethanol yield and both the degree of straw delignification and the alkali level was observed. At optimum delignified straw concentration (4% w/v), a maximum ethanol yield of 0·275 g ethanol g−1 of straw was obtained corresponding to 67·8% of the theoretical yield.
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| 12. |
- Christakopoulos, Paul, et al.
(författare)
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Direct fermentation of cellulose to ethanol by Fusarium oxysporum
- 1989
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Ingår i: Enzyme and microbial technology. - : Elsevier BV. - 0141-0229 .- 1879-0909. ; 11:4, s. 236-239
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Tidskriftsartikel (refereegranskat)abstract
- The cellulase hyperproducing strain F3 of Fusarium oxysporum fermented glucose, xylose, cellobiose, and cellulose directly to ethanol. Conversion of cellulose to ethanol was markedly affected by the pH of both aerated preculture and nonaerated fermentation. Optimum values of cellulose conversion to ethanol were obtained when aerated and nonaerated processes were carried out at pH 5.5 and 6, respectively. Maximum ethanol concentrations of 9.6 and 14.5 g l−1, corresponding to 89.2 and 53.2% of the theoretical yield, were obtained when the fungus was grown under nonaerated conditions at 34°C for 6 days in a medium containing 20 and 50 g l−1cellulose, respectively.
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| 13. |
- Christakopoulos, Paul, et al.
(författare)
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Enhanced acetyl esterase production by Fusarium oxysporum
- 1999
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Ingår i: World Journal of Microbiology & Biotechnology. - 0959-3993 .- 1573-0972. ; 15:4, s. 443-446
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Tidskriftsartikel (refereegranskat)abstract
- Production of acetyl esterase (EC 3.1.1.6) by Fusarium oxysporum strain F3 was enhanced by optimization of growth conditions. Under optimal conditions, activities as high as 0.89 U/ml of culture medium were obtained. The culture filtrate was equally active on p-nitrophenyl acetate and acetylxylan. The enzyme produced 71% deacetylation of acetylxylan in 2 h at 40 ∘C. Activity was optimized at pH6.5 and at 55 ∘C. The respective Km values for p-nitrophenyl acetate and acetylxylan were 0.25 mM and 1.05% (w/v) and the Vm values were 0.65 and 0.43 μmol acetate/min/mg protein.
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| 14. |
- Christakopoulos, Paul, et al.
(författare)
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Enhancement of pH-stability of a low molecular mass endoglucanase from Fusarium oxysporum by protein pegylation
- 1998
-
Ingår i: Carbohydrate Research. - 0008-6215 .- 1873-426X. ; 314:1-2, s. 95-99
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Tidskriftsartikel (refereegranskat)abstract
- The stability of the low molecular mass endoglucanase (23.2 kDa) from Fusarium oxysporum at alkaline pH was enhanced by chemical modification. Two distinct types of amino acid-specific modifiers were used. The first, either cyanuric chloride activated polyethylene glycol (CC–PEG) or polyethylene glycol succinimidyl succinate active ester (SS–PEG), react (more or less specifically) with protein amino groups. The second type, maleimide polyethylene glycol (Mal–PEG), is specific for cysteinyl residues. The enzyme lost almost all of its activity when modified with CC–PEG, whereas no inactivation was observed with SS–PEG and Mal–PEG. The modified endoglucanase showed remarkably enhanced alkaline pH stability. When acting upon cello-oligosaccharides and 4-methylumbelliferyl cello-oligosaccharides, the enzyme preferentially cleaved the internal glycosidic bonds. The modified enzymes mediated a decrease in the viscosity of carboxymethyl cellulose (CMC) associated with the release of only small amounts of reducing sugar. Thus, the modified enzyme retains the endo character of the native enzyme
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| 15. |
- Christakopoulos, Paul, et al.
(författare)
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Exceptionally thermostable α- and β-galactosidase from Aspergillus niger separated in one step
- 1990
-
Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 25:6, s. 210-212
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Tidskriftsartikel (refereegranskat)abstract
- Extracellular alpha- and-beta-galactosidases from a strain of Aspergillus niger were separated and purified in one step by cation exchange chromatography. Both enzymes had acidic pH (3.5-4.0) and high temperature (65-degrees-C) optima and an exceptionally high thermostability. Thus, -alpha-galactosidase had an activity half-time of 104 min at 60-degrees-C whereas at the same temperature the respective value for-beta-galactosidase was 835 min. At optimum conditions of activity the apparent K(m) values of alpha- and beta-galactosidase were 0.44mM and 1.1mM respectively. Both the high temperature optima and thermostability properties of the enzymes make them particularly suitable for high temperature processes.
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| 16. |
- Christakopoulos, Paul, et al.
(författare)
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Functional characterization of a cellulose binding xylanase from Fusarium oxysporum
- 1996
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 18:3, s. 349-354
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Tidskriftsartikel (refereegranskat)abstract
- An extracellular endoxylanase from Fusarium oxysporum binds onto crystalline cellulose. A small peptide (~ 2kDa) could be isolated after partial proteolysis of the native protein. It consists of 18 amino acids, is located in the C-terminal region of the protein and corresponds functionally to a cellulose binding domain (CBD), the first one to be reported in a fungal xylanase. The amino acid sequence of this peptide shows no homology with any known CBD
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| 17. |
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| 18. |
- Christakopoulos, Paul, et al.
(författare)
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On the mechanism of direct conversion of cellulose to ethanol by Fusarium oxysporum : Effect of cellulase and β-glucosidase
- 1990
-
Ingår i: Applied Microbiology and Biotechnology. - 0175-7598 .- 1432-0614. ; 33:1, s. 18-20
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Tidskriftsartikel (refereegranskat)abstract
- The effects of the three main enzymes involved in cellulose saccharification, namely cellobiohydrolase, carboxymethylcellulase and beta-glucosidase, on the direct conversion of cellulose to ethanol by Fusarium oxysporum F3 were investigated. Ethanol production was not affected when the activity of the former two enzymes was varied within a wide range. By contrast, beta-glucosidase markedly affected ethanol production showing an optimum level of 0.7-0.8 unit/ml growth medium. A significant decrease of cellulose bioconversion time to ethanol was obtained when beta-glucosidase activity was adjusted to this optimal level at the beginning of the fermentation process.
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| 19. |
- Christakopoulos, Paul, et al.
(författare)
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Optimization of β-glucosidase catalysed synthesis of trisaccharides from cellobiose and gentiobiose
- 1994
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 16:6, s. 587-592
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Tidskriftsartikel (refereegranskat)abstract
- Purified β-Glucosidase from Fusarium oxysporum catalysed the hydrolysis and transglycosylation reactions in the presence of cellobiose and gentiobiose. The product of the latter reaction was mainly a triose. The time of incubation, pH and substrate concentration for transglycosylation reaction were optimised. Under optimal conditions, the concentration of glucose and triose reached approximately 15–20 % of the initial substrate concentration. These results suggested that β-glucosidase from F.oxysporum is an ideal enzyme for the synthesis of triose in reasonable quantities.
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| 20. |
- Christakopoulos, Paul, et al.
(författare)
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Production and characterization of extracellular lipase from Calvatia gigantea
- 1992
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Ingår i: Applied Microbiology and Biotechnology. - 0175-7598 .- 1432-0614. ; 38:2, s. 194-197
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Tidskriftsartikel (refereegranskat)abstract
- A number of factors affecting production of extracellular lipase by the edible fungus Calvatia gigantea were investigated. Consecutive optimization of carbon and nitrogen sources, initial pH of culture medium and growth temperature resulted in an increase in lipase activity of 87%. Under optimum conditions, activities as high as 22.4 units ml−1 of culture medium were obtained, competing favourably with most activities reported for other lipase hyperproducing microorganisms. The enzyme was optimally active at pH 7.0 and 30°C and had, at optimum pH, half-lives of 75.7 and 22.9 min at 45 and 55°C. Both high activity and kinetic characteristics of the enzyme make this process worthy of further investigation.
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| 21. |
- Christakopoulos, Paul, et al.
(författare)
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Production of an esterase from Fusarium oxysporum catalysing transesterification reactions in organic solvents
- 1998
-
Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 33:7, s. 729-733
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Tidskriftsartikel (refereegranskat)abstract
- The production of an esterase by Fusarium oxysporum, grown on tomato skins as the sole carbon source, was studied in submerged and solid state cultures. Under optimum growth conditions, enzyme yields as high as 7·3 U/ml of culture medium and 19·4 U/g of carbon source were obtained. The esterase catalysed the synthesis of esters in organic solvents. Geraniol was transacetylated in hexane by the esterase using triacetyl as an acetyl donor. The geranyl acetate yield was 68%.
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| 22. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and characterisation of a major xylanase with cellulase and transferase activities from Fusarium oxysporum
- 1996
-
Ingår i: Carbohydrate Research. - : Elsevier BV. - 0008-6215 .- 1873-426X. ; 289, s. 91-104
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Tidskriftsartikel (refereegranskat)abstract
- A major xylanase from Fusarium oxysporum was purified to homogeneity by gel filtration, affinity, and ion-exchange chromatographies. It has a molecular mass of 60.2 kDa and pl of 6.6 and was optimally active at pH 7.4 and at 50 °C. The enzyme was stable over the pH range 5.8–8.2 at 40 °C for 24 h and lost 45% of its original activity at pH 9.0 under the identical conditions. The enzyme rapidly hydrolysed xylans from oat spelts (husks) and birchwood, but the activities on carboxymethylcellulose (CMC), filter paper, and Avicel were very low. Determination of kcat/Km revealed that the enzyme hydrolysed oat spelts and birchwood xylans, 15–30 times more efficiently than CMC. In a 24 h incubation, at pH 7.0 and 9.0, the enzyme hydrolysed oat spelts and birchwood xylans by 75 and 65%, respectively. However, at pH 7.0, the enzyme released almost equal amounts of xylose and xylobiose from both xylans, whereas at pH 9.0, the concentration of xylobiose was twice as muchi as that of xylose and xylotriose. Xylanase attacked preferentially the internal glycosidic bonds of xylo- and 4-methylumbelliferyl cello-oligosaccharides [MeUmb(Glc)n]. The enzyme catalysed transglycosylation reaction with xylotriose, xylotetraose, and xylopentaose as donors and 4-methylumbelliferyl β-d-glucoside (MeUmbGlc) as an acceptor.
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| 23. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and Characterisation of an Extracellular β-Glucosidase with Transglycosylation and Exo-glucosidase Activities from Fusarium oxysporum
- 1994
-
Ingår i: European Journal of Biochemistry. - : Wiley. - 0014-2956 .- 1432-1033. ; 224:2, s. 379-385
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Tidskriftsartikel (refereegranskat)abstract
- An extracellular β-glucosidase from Fusarium oxysporum was purified to homogeneity by gel-filtration and ion-exchange chromatographies. The enzyme, a monomeric protein of 110 kDa, was maximally active at pH 5.0–6.0 and at 60°C. It hydrolysed 1→4-linked aryl-β-glucosides and 1→4-linked, 1→3-linked and 1→6–linked β-glucosides. The apparent Km and kcat values for p -nitrophenyl β-d-glucopyranoside (4-NpGlcp) and cellobiose were 0.093 (Km), 1.07 mM (kcat) and 1802 (Km), 461.5 min-1 (kcat), respectively. Glucose and gluconolactone inhibited the enzyme competitively with Ki values of 2.05 mM and 3.03 μM, respectively. Alcohols activated the enzyme; butanol showed maximum effect (2.2-fold at 0.5 M) while methanol increased the activity by 1.4-fold at 1 M. The enzyme catalysed the synthesis of methylglucosides, ethylglucoside and propylglucosides, as well as trisaccharides in the presence of different alcohols and disaccharides, respectively. In addition, the enzyme hydrolysed the unsubstituted and methylumbelliferyl cello-oligosaccharides [MeUmb(Glc)n] but the rate of hydrolysis decreased with increasing chain length. Analysis of products released from MeUmb(Glc)n as a function of time revealed that the enzyme attacked these substrates in a stepwise manner and from both ends. Thus, β-glucosidase from F. oxysporum, with the above interesting properties, could be of commercial interest.
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| 24. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and characterization of a less randomly acting endo-1,4-beta-D-glucanase from the culture filtrates of Fusarium oxysporum
- 1995
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Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861 .- 1096-0384. ; 316:1, s. 428-433
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Tidskriftsartikel (refereegranskat)abstract
- An extracellular endo-1,4-β-D-glucanase from Fusarium oxysporum was purified by affinity chromatography and gel filtration. The enzyme purified in this way was homogeneous when judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and isoelectric focusing-polyacrylamide gel electrophoresis. The protein corresponded to a molecular mass and pI value of 41.7 kDa and 6.4, respectively. It was optimally active at pH 4.5 and at 55°C. The enzyme hydrolyzed carboxymethylcellulose (CMC) and unsubstituted and substituted cello-oligosaccharides but was inactive on Avicel, filter paper, xylan, cellobiose, p-nitrophenyl-β-D-glucoside, and p-nitrophenyl-β-D-xyloside. However, the enzyme effected only a small change in viscosity of CMC per unit increase of reducing sugar. When cellotriose, cellotetraose, and cellopentaose were used as substrates, the enzyme released mainly cellobiose. Use of 4-methylumbelliferyl cello-oligosaccharides and the determination of bond cleavage frequency revealed that the enzyme preferentially hydrolyzed the glycosidic bond adjacent to 4-methylumbelliferone. Thus, the purified enzyme appeared to be a less randomly acting endoglucanase.
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| 25. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and characterization of an extracellular α-L- arabinofuranosidase from Fusarium oxysporum
- 2000
-
Ingår i: Applied Biochemistry and Biotechnology. - 0273-2289 .- 1559-0291. ; 87:2, s. 127-133
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Tidskriftsartikel (refereegranskat)abstract
- An α-L-arabinofuranosidase from Fusarium oxysporum F3 was purified to homogeneity by a two-step ion exchange intercalated by a gel filtration chromatography. The enzyme had a molecular mass of 66 kDa and was optimally active at pH 6.0 and 60°C. It hydrolyzed aryl α-L-arabinofuranosides and cleaved arabinosyl side chains from arabinoxylan and arabinan. There was a marked synergistic effect between the α-L-arabinofuranosidase and an endo-(1→4)-β-D-xylanase produced by F. oxysporum in the extensive hydrolysis of arabinoxylan.
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| 26. |
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| 27. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and mode of action of a low molecular mass endo-1,4-β-d-glucanase from Fusarium oxysporum
- 1995
-
Ingår i: Journal of Biotechnology. - : Elsevier BV. - 0168-1656 .- 1873-4863. ; 39:1, s. 85-93
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Tidskriftsartikel (refereegranskat)abstract
- A low molecular mass (23.2 kDa) endo-1,4-β-d-glucanase from Fusarium oxysporum was purified to homogeneity by gel-filtration and ion-exchange chromatographies. The enzyme was optimally active at pH 6.0 and at 50 ° C. It had a pI value of 8.6 and was stable at 55 ° C for 1 h. It hydrolyzed carboxymethylcellulose, cello-oligosaccharides (Glcn) and 4-methylumbelliferylcello-oligosaccharides but did not hydrolyze cellobiose, p-nitrophenyl β-o-glucoside, p-nitrophenyl β-d-xyloside, Avicel, filter paper and xylan. Analysis of reaction mixtures by high pressure liquid chromatography revealed that this enzyme cleaved preferentially the internal glycoside bonds of higher cello-oligosaccharides. The enzyme also catalyzed the formation of transfer products in the presence of cellotriose, cellotetraose and 4-methylumbelliferylglucoside (MeUmbGlc).
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| 28. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and mode of action of an alkali-resistant endo-1,4-β-glucanase from Bacillus pumilus
- 1999
-
Ingår i: Archives of Biochemistry and Biophysics. - : Elsevier BV. - 0003-9861 .- 1096-0384. ; 364:1, s. 61-66
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Tidskriftsartikel (refereegranskat)abstract
- Alkaline endo-1,4-β-d-glucanase was secreted byBacillus pumilusgrown in submerged culture on a combination of oat spelt xylan and corn starch as carbon sources. The enzyme was purified to homogeneity by Sephacryl S-200 and Q-Sepharose column chromatography. The protein corresponded to molecular mass and pIvalues of 67 kDa and 3.7, respectively. The enzyme was optimally active at pH 7.0–8.0 and 60°C and retained 50% of its optimum activity at pH 12. The most notable characteristic of the endoglucanase was its high stability up to pH 12 for 20 h at 30°C. The enzyme hydrolyzed carboxymethylcellulose (CMC) and cello-oligosaccharides but was inactive on cellobiose, cellotriose, Avicel, xylan, 4-nitrophenyl-β-d-glucoside, 4-nitrophenyl-β-d-cellobioside, and 4-nitrophenyl-β-d-xyloside. Analysis of reaction mixtures by HPLC revealed that the enzyme produced almost exclusively cellotriose when acted on CMC and appeared to hydrolyze cello-oligosaccharides by successively releasing cellotriose. The use of 4-methylumbelliferyl cello-oligosaccharides and the determination of bond cleavage frequency revealed that the enzyme preferentially hydrolyzed the third glycosidic bond adjacent to the glycon. The enzyme mediated a decrease in the viscosity of CMC associated with a release of only small amounts of reducing sugar. The enzyme activity was not inhibited by metal ions, surfactants, and chelating agents used as components of laundry detergents.
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| 29. |
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| 30. |
- Hatzinikolaou, D.G, et al.
(författare)
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Comparative growth studies of the extreme thermophile Sulfolobus acidocaldarius in submerged and solidified substrate cultures
- 2001
-
Ingår i: World Journal of Microbiology & Biotechnology. - 0959-3993 .- 1573-0972. ; 17:3, s. 229-234
-
Tidskriftsartikel (refereegranskat)abstract
- An attempt was made, for the first time, to exploit cultures on solidified substrates (SSC) as an alternative to submerged cultures (SmC) for growing extremophilic micro-organisms. The extreme thermophilic archaebacterium Sulfolobus acidocaldarius was grown on a number of carbon sources and, in all experiments, biomass yields and growth rates were always higher in SSC than in the corresponding SmC. Inoculum age significantly affected growth characteristics on both types of fermentation. Heavy growth of the micro-organism in SSC was observed on low-cost carbon sources such as starch. Wheat bran significantly enhanced growth characteristics when used to supplement starch media. The results of this work show that cultures on solid surfaces could be a promising alternative method for growing extreme thermophiles.
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| 31. |
- Hatzinikolaou, D.G, et al.
(författare)
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Production and partial characterisation of extracellular lipase from aspergillus niger
- 1996
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Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 18:5, s. 547-552
-
Tidskriftsartikel (refereegranskat)abstract
- The production and certain kinetic characteristics of extracellular lipase from Aspergillus niger were investigated. It was possible to substantially enhance the activity of excreted lipase by optimising the interaction between carbon and nitrogen sources applying a two-parameter complete experimental design and response surface analysis. The enzyme was partially purified and a number of kinetic characteristics such as optimum pH and temperature, thermal and pH stability and K(m) were determined and discussed. The elevated levels of lipase activity (40.5 U/ml) found in this work competed favourably with most of those reported for lipase hyperproducing fungi.
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| 32. |
- Kalogeris, E, et al.
(författare)
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Catalytic properties of the endoxylanase I from Thermoascus aurantiacus
- 2001
-
Ingår i: Journal of Molecular Catalysis B. - 1381-1177 .- 1873-3158. ; 11:4-6, s. 491-501
-
Tidskriftsartikel (refereegranskat)abstract
- Endo-β-1,4-xylanase I previously purified from Thermoascus aurantiacus solid state culture was further characterized. The enzyme had a molecular weight of 33 kDa by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and 31 kDa by gel filtration. Thin layer chromatography (TLC) analysis showed that endoxylanase liberates aldotetrauronic acid MeGlcAα-1,2-Xylβ-1,4-Xylβ-1,4-Xyl as the shortest acidic fragment from glucuronoxylan and an isomeric xylotriose (Xyl3) of the structure Xylβ1-3Xylβ1-4Xyl from rhodymenan. The enzyme performed ideally on O-acetyl-4-O-methylglucuronoxylan, liberating large amounts of short acetylated and non-acetylated fragments. Also, the enzyme was capable to hydrolyse arabinoxylan to arabinose (Arab), xylose (Xyl) and xylobiose (Xyl2). The enzyme degraded pNPX (4-nitrophenyl β-D-xylopyranoside) by a complex reaction pathway that involved both hydrolysis and glycosyl transfer reactions. The enzyme tolerates the replacement of β-xylopyranosyl units in several artificial substrates by β-glucopyranosyl, α-L-arabinopyranosyl and α-L-arabinofuranosyl units and was active on pNPC (4-nitrophenyl β-D-cellobioside), pNP-Arap (4-nitrophenyl α-L-arabinopyranoside) and pNPAraf (4-nitrophenyl α-L-arabinofuranoside). The enzyme also hydrolysed the 4-methylumbelliferyl glycosides of β-D-xylobiose and β-D-xylotriose at the agluconic linkage. The results suggested that the xylanase I from T. aurantiacus has catalytic properties similar to those belonging to family 10. Copyright © 2001 Elsevier Science B.V.
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| 33. |
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| 34. |
- Kalogeris, E, et al.
(författare)
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Performance of an intermittent agitation rotating drum type bioreactor for solid-state fermentation of wheat straw
- 2003
-
Ingår i: Bioresource Technology. - 0960-8524 .- 1873-2976. ; 86:3, s. 207-213
-
Tidskriftsartikel (refereegranskat)abstract
- A laboratory bioreactor, designed for solid-state fermentation of thermophilic microorganisms, was operated for production of cellulases and hemicellulases by the thermophilic fungus Thermoascus aurantiacus. The suitability of the apparatus for the effective control of important operating variables affecting growth of microbes in solid-state cultivation was determined. Application of the optimum conditions found for the moisture content of the medium, growth temperature and airflow rate produced enzyme yields of 1709 U endoglucanase, 4 U cellobiohydrolase, 79 U β-glucosidase, 5.5 U FPA, 4490 U xylanase and 45 U β-xylosidase per g of dry wheat straw. The correlation between microorganism growth and production of enzymes was efficiently described by the Le Duy kinetic model. © 2002 Elsevier Science Ltd. All rights reserved.
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| 35. |
- Kalogeris, E, et al.
(författare)
-
Production and characterization of cellulolytic enzymes from the thermophilic fungus Thermoascus aurantiacus under solid state cultivation of agricultural wastes
- 2003
-
Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 38:7, s. 1099-1104
-
Tidskriftsartikel (refereegranskat)abstract
- Extracellular cellulolytic enzymes were produced under solid state cultivation by the thermophilic fungus Thermoascus aurantiacus and characterized. Elevated levels of endoglucanase and β-glucosidase activities were produced simultaneously by optimization of growth factors. Under optimal growth conditions, 1572 U endoglucanase and 101.6 U β-glucosidase per g of carbon source were obtained. Chromogenic (fluorogenic) 4-methylumbelliferyl-β-glycosides of glucose (MUG) and cellobiose (MUG2) were used to characterize the cellulolytic multienzyme components after separation by isoelectric focusing. The zymogram indicated one endoglucanase and one β-glucosidase with pI values 3.5 and 3.9, respectively. Both enzymes exhibited significant thermostability, with half-lives of 42 and 18 min, respectively, at 80°C
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| 36. |
- Kalogeris, E., et al.
(författare)
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Studies on the solid-state production of thermostable endoxylanases from Thermoascus aurantiacus : Characterization of two isozymes
- 1998
-
Ingår i: Journal of Biotechnology. - 0168-1656 .- 1873-4863. ; 60:3, s. 155-163
-
Tidskriftsartikel (refereegranskat)abstract
- Production of xylanases by the thermophilic fungus Thermoascus aurantiacus under solid state culture (SSC) was enhanced by optimization of the type of carbon and nitrogen source, inoculum type, moisture level and particle size of the carbon source. Under these conditions, yields as high as 6193 U g−1 of carbon source were obtained. Chromogenic (fluorogenic) 4-methylumbelliferyl-β-glycosides of xylose (MUX) and xylobiose (MUX2) were used to characterize xylanase multienzyme components, after separation by isoelectric focusing. The zymogram indicated one major and two minor xylanases and one β-xylosidase. The major (xylanase I) and one of the minor (xylanase II) xylanases were separated and characterized. Both xylanases exhibited remarkable thermostability.
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| 37. |
- Katapodis, Petros, et al.
(författare)
-
Biochemical and catalytic properties of an endoxylanase purified from the culture filtrate of Sporotrichum thermophile
- 2003
-
Ingår i: Carbohydrate Research. - 0008-6215 .- 1873-426X. ; 338:18, s. 1881-1890
-
Tidskriftsartikel (refereegranskat)abstract
- An endo-β-1,4-xylanase (1,4-β-d-xylan xylanoxydrolase, EC 3.2.1.8) present in culture filtrates of Sporotrichum thermophile ATCC 34628 was purified to homogeneity by Q-Sepharose and Sephacryl S-200 column chromatographies. The enzyme has a molecular mass of 25,000 Da, an isoelectric point of 6.7, and is optimally active at pH 5 and at 70 °C. Thin-layer chromatography (TLC) analysis showed that endo-xylanase liberates mainly xylose (Xyl) and xylobiose (Xyl2) from beechwood 4-O-methyl-d-glucuronoxylan, O-acetyl-4-O-methylglucuronoxylan and rhodymenan (a β-(1→4)-β(1→3)-xylan). Also, the enzyme releases an acidic xylo-oligosaccharide from 4-O-methyl-d-glucuronoxylan, and an isomeric xylotetraose and an isomeric xylopentaose from rhodymenan. Analysis of reaction mixtures by high performance liquid chromatography (HPLC) revealed that the enzyme cleaves preferentially the internal glycosidic bonds of xylooligosaccharides, [1-3H]-xylooligosaccharides and xylan. The enzyme also hydrolyses the 4-methylumbelliferyl glycosides of β-xylobiose and β-xylotriose at the second glycosidic bond adjacent to the aglycon. The endoxylanase is not active on pNPX and pNPC. The enzyme mediates a decrease in the viscosity of xylan associated with a release of only small amounts of reducing sugar. The enzyme is irreversibly inhibited by series of ω-epoxyalkyl glycosides of d-xylopyranose. The results suggest that the endoxylanase from S. thermophile has catalytic properties similar to the enzymes belonging to family 11.
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| 38. |
- Katapodis, P., et al.
(författare)
-
Biosynthesis of fructo-oligosaccharides by Sporotrichum thermophile during submerged batch cultivation in high sucrose media
- 2004
-
Ingår i: Applied Microbiology and Biotechnology. - : Springer Science and Business Media LLC. - 0175-7598 .- 1432-0614. ; 63:4, s. 378-382
-
Tidskriftsartikel (refereegranskat)abstract
- A feruloyl esterase (StFAE-A) produced by Sporotrichum thermophile was purified to homogeneity. The purified homogeneous preparation of native StFAE-A exhibited a molecular mass of 57.0±1.5 kDa, with a mass of 33±1 kDa on SDS-PAGE. The pI of the enzyme was estimated by cation-exchange chromatofocusing to be at pH 3.1. The enzyme activity was optimal at pH 6.0 and 55–60 °C. The purified esterase was stable at the pH range 5.0–7.0. The enzyme retained 70% of activity after 7 h at 50 °C and lost 50% of its activity after 45 min at 55 °C and after 12 min at 60 °C. Determination of k cat/K m revealed that the enzyme hydrolyzed methyl p-coumarate 2.5- and 12-fold more efficiently than methyl caffeate and methyl ferulate, respectively. No activity on methyl sinapinate was detected. The enzyme was active on substrates containing ferulic acid ester linked to the C-5 and C-2 linkages of arabinofuranose and it hydrolyzed 4-nitrophenyl 5-O-trans-feruloyl-α-l-arabinofuranoside (NPh-5-Fe-Araf) 2-fold more efficiently than NPh-2-Fe-Araf. Ferulic acid (FA) was efficiently released from destarched wheat bran when the esterase was incubated together with xylanase from S. thermophile (a maximum of 34% total ferulic acid released after 1 h incubation). StFAE-A by itself could release FA, but at a level almost 47-fold lower than that obtained in the presence of xylanase. The potential of StFAE-A for the synthesis of various phenolic acid esters was tested using a ternary water-organic mixture consisting of n-hexane, 1-butanol and water as a reaction system.
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| 39. |
- Katapodis, Petros, et al.
(författare)
-
Enzymic production of a feruloylated oligosaccharide with antioxidant activity from wheat flour arabinoxylan
- 2003
-
Ingår i: European Journal of Nutrition. - : Springer Science and Business Media LLC. - 1436-6207 .- 1436-6215. ; 42:1, s. 55-60
-
Tidskriftsartikel (refereegranskat)abstract
- Background Main cereals such as rice, wheat, barley, and corn belong to the family Gramineae and have similar cell-wall composition. Since cereal cell walls are a good source of dietary fibre, meeting one-half of the daily requirement of 30 g of dietary fibre can be achieved by the regular consumption of cereals. Many studies have dealt with the isolation of feruloylated oligosaccharides from Gramineae by treatment with polysaccharide hydrolysing enzymes. Aim of this study Therefore, the purpose of this study was to investigate the production of feruloylated oligosaccharides from insoluble wheat flour arabinoxylan (WFAX) by treatment with a Thermoascus aurantiacus family 10 endoxylanase (XYLI) and the evaluation of their antioxidant activity. Methods The main feruloylated oligosaccharide was purified by anion-exchange and size-exclusion chromatography (SEC). Alkaline saponification and acid hydrolysis were used for product identification. Evaluation of antioxidant activity was performed by the 2,2-diphenyl-1-picrylhydrazyl (DPPH) reduction assay and the inhibition of copper-mediated oxidation of low density lipoprotein (LDL). Results The optimal conditions for WFAX hydrolysis using the XYLI have been determined to be 100 U g(-1) of WFAX for 30 min at 50 degreesC. Saponification of the oligosaccharide released FA and oligosaccharide. The released oligosaccharide consisted of arabinose and xylose in a molar ratio of 1:3 and these results support the identity of the feruloylated oligosaccharide as feruloyl arabinoxylotrisaccharide (FAX(3)). FAX(3) showed profound antioxidant activity in 2,2-diphenyl-1-picrylhydrazyl (DPPH) reduction assay exhibiting an antiradical efficiency of 0.035 (x 10(-3)) and inhibited the copper-mediated oxidation of human low density lipoprotein (LDL) in a dose-dependent manner with almost complete inhibition at 32 muM. Conclusion A feruloylated oligosaccharide (FAX(3)) was isolated from WFAX after enzymatic treatment with XYLI. We verified antioxidant activity of FAX(3) which may be important in preventing or reducing the progression of atherosclerosis by inhibiting the peroxidation of lipoproteins.
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| 40. |
- Katapodis, Petros, et al.
(författare)
-
Enzymic production of aldopentauronic acid and use as bioregulator in plant airlift bioreactors
- 2003
-
Ingår i: Journal of Bioscience and Bioengineering. - 1389-1723 .- 1347-4421. ; 95:6, s. 630-632
-
Tidskriftsartikel (refereegranskat)abstract
- Neutral and acidic oligosaccharides were obtained from birchwood xylan by treatment with an endoxylanase, family 11 class, from Sporotrichum thermophile. The main acidic xylooligosaccharide (aldopentauronic acid) was separated from the hydrolysate by anion-exchange and size-exclusion chromatography and the structure was determined by 13C NMR spectroscopy. The aldopentauronic acid yield was 25% (w/w) of the total solubilized sugars. The addition of purified aldopentauronic acid at a concentration of 5 mg/l to cucumber liquid culture in 2.5-l airlift bioreactors caused in increase in both the number of regenerants and their fresh weight.
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| 41. |
- Katapodis, P, et al.
(författare)
-
Production of acidic xylo-oligosaccharides by a family 10 endoxylanase from Thermoascus aurantiacus and use as plant growth regulators
- 2002
-
Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 24:17, s. 1413-1416
-
Tidskriftsartikel (refereegranskat)abstract
- Neutral and acidic oligosaccharides were obtained from birchwood xylan by treatment with an endoxylanase, family 10 class, from Thermoascus aurantiacus. The main acidic xylooligosaccharide (aldotetrauronic acid) was separated from the hydrolysate by anion-exchange and size-exclusion chromatography and the primary structure was determined by 13C NMR spectroscopy. The aldotetrauronic yield was 15% (w/w) of the total solubilised sugars. The addition of purified aldoterauronic acid at 1.6-16 mg 1 -1 growth medium, induced callus and somatic embryogenesis in culture explants of common mallow (Malva silvestris L.) and cotton (Gosssypium hirsutum).
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| 42. |
- Katapodis, Petros, et al.
(författare)
-
Production of β-Fructofuranosidase from Sporotrichum thermophile and Its Application in the Synthesis of Fructooligosaccharides
- 2003
-
Ingår i: Food biotechnology. - 0890-5436 .- 1532-4249. ; 17:1, s. 1-14
-
Tidskriftsartikel (refereegranskat)abstract
- Production of β-fructofuranosidase from the thermophilic fungus Sporotrichum thermophile was studied. The effect of nitrogen source, as well as the type and concentration of carbon source on enzyme production was examined. The results from flask experiments were used for the production of the enzyme in 7-l bioreactors. β-Fructofuranosidase from Sporotrichum thermophile showed both transfructosylating and hydrolytic activities. It was optimally active at 60°C, while the optimal pHs for hydrolysis and transfructosylation were 4.0 and 6.0, respectively. Synthesis of fructooligosaccharides was maximized at 20% (w/v) initial sucrose concentration. The major sugar produced by the transfructosylating activity of the enzyme was 6-kestose
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| 43. |
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| 44. |
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| 45. |
- Koullas, D.P., et al.
(författare)
-
Effect of alkali delignification on wheat straw saccharification by fusarium oxysporum cellulases
- 1993
-
Ingår i: Biomass and Bioenergy. - 0961-9534 .- 1873-2909. ; 4:1, s. 9-13
-
Tidskriftsartikel (refereegranskat)abstract
- The effect of alkaline delignification of wheat straw on the chemical composition and the subsequent enzymic hydrolysis of the pretreated straw are reported. Both hot (120°°C) and cold (20–36°°C) delignification were investigated, using either aqueous or organic alkaline solutions. The treated lignocellulosic materials were hydrolyzed by the cellulases of Fusarium oxysporum strain F3. Both delignification and saccharification yield showed linear relationships with the level of alkali used. Under the chosen experimental conditions 70–100% hydrolysis was achieved either by hot or cold delignification. Delignification to at least 50% appeared crucial for total polysaccharide conversion.
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| 46. |
- Lezinou, V., et al.
(författare)
-
Simultaneous saccharification and fermentation of sweet sorghum carbohydrates to ethanol in a fed-batch process
- 1994
-
Ingår i: Biotechnology letters. - 0141-5492 .- 1573-6776. ; 16:9, s. 983-988
-
Tidskriftsartikel (refereegranskat)abstract
- The simultaneous saccharification and fermentation (SSF) of sweet sorghum carbohydrates to ethanol by Fusarium oxysporum F3 alone or in mixed culture with Saccharomyces cerevisiae 2541 or Zymomonas mobilis CP4 in a fed-batch fermentation process was studied. While SSF was adequately carried out by the first microorganism the process achieved its maximum value by the mixed culture of the fungus and yeast. Under optimum conditions, ethanol yields and concentrations as high as 29.7 g of ethanol per 100 g of dry sorghum stalk and 7.5 % (w/v) respectively were obtained. These values together with the high yield of sorghum crop in Greece make this process promising and worthy of further investigation for the production of fuel bioethanol
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| 47. |
- Lezinou, V., et al.
(författare)
-
Study of a single and mixed culture for the direct bio-conversion of sorghum carbohydrates to ethanol
- 1995
-
Ingår i: Applied Microbiology and Biotechnology. - 0175-7598 .- 1432-0614. ; 43:3, s. 412-415
-
Tidskriftsartikel (refereegranskat)abstract
- Fusaium oxysporum F3 alone or in mixed culture with Saccharomyces cerevisiae 2541 fermented soluble and insoluble carbohydrates of sweet sorghum stalk directly to ethanol. Both microorganisms were first grown aerobically and fermented sorghum stalk to ethanol thereafter. During fermentation, insoluble carbohydrates were hydrolysed to soluble sugars by the celluloytic system of F. oxysporum. Ethanol yields as high as 24.4 and 33.5 g/100 g dry stalks were obtained by F. oxysporum and the mixed culture respectively, representing a theoretical yield enhancement of 11.6% and 53.6% respectively. The corresponding ethanol concentrations in the fermentation medium were 4.6% and 6.4% (w/v). These results clearly demonstrated that a large portion of insoluble carbohydrate from sorghum was converted by simultaneous saccharification and fermentation to ethanol, making the process promising for bioethanol production.
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| 48. |
- Makropoulou, M., et al.
(författare)
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Factors affecting the specificity of beta-glucosidase from Fusarium oxysporum in enzymatic synthesis of alkyl-beta-D-glucosides
- 1998
-
Ingår i: International Journal of Biological Macromolecules. - 0141-8130 .- 1879-0003. ; 22:2, s. 97-101
-
Tidskriftsartikel (refereegranskat)abstract
- Factors affecting the specificity of β-glucosidase from Fusarium oxysporum in enzymatic synthesis of alkyl-β-d-glucosidesFusarium oxysporumβ-glucosidase has been used to catalyze the production of alkyl-β-d-glucosides from various disaccharides, based on the transglucosylation reaction, in the presence of primary, secondary and tertiary alcohols as glucosyl acceptors. Primary alcohols were found to be the best acceptors. The influence of the glucosyl donor concentration, as well as the enzyme specificity towards the cleaved glucosidic bond and the aglucone part of the donor, have also been investigated. The enzyme does not exhibit regiospecificity and seems to be unspecific towards the aglucone part. The specificity of the β linkage has been confirmed by proton nuclear magnetic resonance (1H NMR) analysis.
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| 49. |
- Mamma, D., et al.
(författare)
-
An alternative approach to the bioconversion of sweet sorghum carbohydrates to ethanol
- 1995
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Ingår i: Biomass and Bioenergy. - 0961-9534 .- 1873-2909. ; 8:2, s. 99-103
-
Tidskriftsartikel (refereegranskat)abstract
- The ethanol fermentation of juice and press cake, resulting from the squeezing of sweet sorghum stalks at high pressure, was investigated. The juice was fermented by Saccharomyces cerevisiae and yielded 4.8 g ethanol per 100 g of fresh stalks. The press cake was fermented directly to ethanol by a mixed culture of Fusarium oxysporum and Saccharomyces cerevisiae and yielded 5.1 g ethanol per 100 g of fresh stalks. An overall ethanol concentration and yield of 5.6% (w/v) and 9.9 g of ethanol per 100 g of fresh stalks respectively was obtained. Based on soluble carbohydrates, the ethanol yield from press cake was doubled while the overall theoretical yield was enhanced by 20.7% due to the bioconversion of a significant portion of cell wall polysaccharides to ethanol. The process was found promising for further investigation.
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| 50. |
- Mamma, Diomi, et al.
(författare)
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Biochemical characterization of the multi-enzyme system produced by Penicillium decumbens grown on rutin
- 2004
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Ingår i: Food biotechnology. - 0890-5436 .- 1532-4249. ; 18:1, s. 1-18
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Tidskriftsartikel (refereegranskat)abstract
- Penicillium decumbens produced a set of enzymes, including a monoxygenase and two glycosidases, which degrade rutin, a nontoxic flavonoid glycoside, to water-soluble products. The monoxygenase (quercetinase) cleaves the heterocyclic ring in quercetin, the aglycone part of rutin. The glycosidases (alpha-L-rhamnosidase and beta-glucosidase) hydrolyze the bonds between quercetin and rutinose, and between glucose and rhamnose, the constituent monosaccharides of rutinose. Simultaneous production of the three enzymes was optimized following the examination of a number of culture conditions. Maximum enzyme activities were observed when the fungus was grown at 30 °C with an initial pH of 7.0, using 8.0 g/L rutin and 9.0 g/L di-ammonium hydrogen phosphate as carbon and nitrogen sources, respectively. The enzymes were purified to electrophoretic homogeneity by a series of consecutive chromatographic steps including anion and cation exchange as well as gel filtration. The purified quercetinase revealed an apparent tetrameric structure, with a reduced molecular mass of 45 kDa. alpha-L-Rhamnosidase showed an apparent molecular mass of 58 kDa and the purified beta-glucosidase was a tetramer exhibiting a reduced molecular mass of 120 kDa.
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