| 1. |
- 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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| 2. |
- 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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| 3. |
- Christakopoulos, Paul, et al.
(författare)
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Purification and characterization of an extracellular α-L- arabinofuranosidase from Fusarium oxysporum
- 2000
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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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| 4. |
- Christov, L, et al.
(författare)
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Effects of purified endo-β-1,4-xylanases of family 10 and 11 and acetyl xylan esterases on eucalypt sulfite dissolving pulp
- 2000
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Ingår i: Journal of Biotechnology. - 0168-1656 .- 1873-4863. ; 83:3, s. 231-244
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Tidskriftsartikel (refereegranskat)abstract
- Sulfite dissolving pulp from Eucalyptus grandis contained approximately 3.8% O-acetyl-4-O-methylglucuronoxylan with a molar ratio of xylose:4-O-methylglucuronic acid:acetyl group close to 13.6:1:6.2. The effects produced by purified endo-xylanases from two different glycosyl hydrolase families (family 10 and 11) as well as acetyl xylan esterases were examined and assessed on pulp in relation to their bleaching abilities. The purified endo-xylanases hydrolyzed only a limited portion (less than 30%) of the acetylglucuronoxylan present in the pulp. The enzymes of family 10 produced acetylated xylobiose and xylotriose whereas acetylated xylobiose was not observed among the products released from the pulp by the family 11 xylanases. The esterases however were not capable of deacetylating the acetylated aldouronic acids generated by the xylanases. Regardless of the different mode of action of the endo-xylanases on dissolving pulp, their effect on pulp bleaching was not related to the amount and nature of sugars generated or the glycosyl hydrolase family. No additional brightness gain was obtained when endo-xylanases were used in conjunction with acetyl xylan esterases, suggesting that the latter do not play an important role in biobleaching of eucalypt sulfite dissolving pulps. Copyright (C) 2000 Elsevier Science B.V. Sulfite dissolving pulp from Eucalyptus grandis contained approximately 3.8% O-acetyl-4-O-methylglucuronoxylan with a molar ratio of xylose:4-O-methylglucuronic acid:acetyl group close to 13.6:1:6.2. The effects produced by purified endo-xylanases from two different glycosyl hydrolase families (family 10 and 11) as well as acetyl xylan esterases were examined and assessed on pulp in relation to their bleaching abilities. The purified endo-xylanases hydrolyzed only a limited portion (less than 30%) of the acetylglucuronoxylan present in the pulp. The enzymes of family 10 produced acetylated xylobiose and xylotriose whereas acetylated xylobiose was not observed among the products released from the pulp by the family 11 xylanases. The esterases however were not capable of deacetylating the acetylated aldouronic acids generated by the xylanases. Regardless of the different mode of action of the endo-xylanases on dissolving pulp, their effect on pulp bleaching was not related to the amount and nature of sugars generated or the glycosyl hydrolase family. No additional brightness gain was obtained when endo-xylanases were used in conjunction with acetyl xylan esterases, suggesting that the latter do not play an important role in biobleaching of eucalypt sulfite dissolving pulps.
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| 5. |
- Faulds, C.B., et al.
(författare)
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Synergy between xylanases from glycoside hydrolase family 10 and family 11 and feruloyl esterase in the release of phenolic acids from cereal arabinoxylan
- 2006
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Ingår i: Applied Microbiology and Biotechnology. - : Springer Science and Business Media LLC. - 0175-7598 .- 1432-0614. ; 71:5, s. 622-629
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Tidskriftsartikel (refereegranskat)abstract
- The bioconversion of waste residues (by-products) from cereal processing industries requires the cooperation of enzymes able to degrade xylanolytic and cellulosic material. The type A feruloyl esterase from Aspergillus niger, AnFaeA, works synergistically with (1→4)-β-d-xylopyranosidases (xylanases) to release monomeric and dimeric ferulic acid (FA) from cereal cell wall-derived material. The esterase was more effective with a family 11 xylanase from Trichoderma viride in releasing FA and with a family 10 xylanase from Thermoascus aurantiacus in releasing the 5,5′ form of diferulic acid from arabinoxylan (AX) derived from brewers’ spent grain. The converse was found for the release of the phenolic acids from wheat bran-derived AXs. This may be indicative of compositional differences in AXs in cereals.
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| 6. |
- Gkargkas, Konstantinos, et al.
(författare)
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Studies on a N-acetyl-β-d-glucosaminidase produced by Fusarium oxysporum F3 grown in solid-state fermentation
- 2004
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Ingår i: Process Biochemistry. - 1359-5113 .- 1873-3298. ; 39:11, s. 1599-1605
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Tidskriftsartikel (refereegranskat)abstract
- Fusarium oxysporum F3 produced N-acetyl-β-d-glucosaminidase when grown on wheat bran and chitin as carbon sources in solid-state fermentation. The initial moisture content and pH of growth medium were 65% and 6.0, respectively, and the enzyme yield 23.6 U g−1 carbon source. Two isozymes of N-acetyl-β-d-glucosaminidase, called N-acetyl-β-d-glucosaminidases I and II, were isolated from the culture filtrate of F. oxysporum F3. The filtrate was subjected to ammonium sulphate fractionation followed by anion exchange, gel filtration, hydrophobic interaction and cation exchange chromatography. The optimum pH of isozymes I and II was 5.0 and 6.0, respectively, whereas maximum activity of both isozymes was obtained at 40 °C. The Km of isozymes I and II was 49.6 and 48.6 μM and the Vmax 1.24 and 0.26 μmol mg−1 min−1, respectively, on p-nitrophenyl N-acetyl-β-d-glucosaminide as substrate. The molecular mass of isozymes I and II was calculated to be 67 kDa by SDS–PAGE.
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| 7. |
- Grotkjær, Thomas, et al.
(författare)
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Comparative metabolic network analysis of two xylose fermenting recombinant Saccharomyces cerevisiae strains
- 2005
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Ingår i: Metabolic engineering. - : Elsevier BV. - 1096-7176 .- 1096-7184. ; 7:5-6, s. 437-444
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Tidskriftsartikel (refereegranskat)abstract
- The recombinant xylose fermenting strain Saccharomyces cerevisiae TMB3001 can grow on xylose, but the xylose utilisation rate is low. One important reason for the inefficient fermentation of xylose to ethanol is believed to be the imbalance of redox co-factors. In the present study, a metabolic flux model was constructed for two recombinant S. cerevisiae strains: TMB3001 and CPB.CR4 which in addition to xylose metabolism have a modulated redox metabolism, i.e. ammonia assimilation was shifted from being NADPH to NADH dependent by deletion of gdh1 and over-expression of GDH2. The intracellular fluxes were estimated for both strains in anaerobic continuous cultivations when the growth limiting feed consisted of glucose (2.5 g L−1) and xylose (13 g L−1). The metabolic network analysis with 13C labelled glucose showed that there was a shift in the specific xylose reductase activity towards use of NADH as co-factor rather than NADPH. This shift is beneficial for solving the redox imbalance and it can therefore partly explain the 25% increase in the ethanol yield observed for CPB.CR4. Furthermore, the analysis indicated that the glyoxylate cycle was activated in CPB.CR4.
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| 8. |
- Hatzinikolaou, Dimitris G., et al.
(författare)
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Cell bound and extracellular glucose oxidases from Aspergillus niger BTL : evidence for a secondary glycosylation mechanism
- 2007
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Ingår i: Applied Biochemistry and Biotechnology. - : Springer Science and Business Media LLC. - 0273-2289 .- 1559-0291. ; 142:1, s. 29-43
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Tidskriftsartikel (refereegranskat)abstract
- Two glucose oxidase (GOX) isoforms where purified to electrophoretic homogeneity from the mycelium extract (GOXI) and the extracellular medium (GOXII) of Aspergillus niger BTL cultures. Both enzymes were found to be homodimers with nonreduced molecular masses of 148 and 159 kDa and pI values of 3.7 and 3.6 for GOXI and GOXII, respectively. The substrate specificity and the kinetic characteristics of the two GOX forms, as expressed through their apparent Km values on glucose, as well as pH and T activity optima, were almost identical. The only structural difference between the two enzymes was in their degrees of glycosylation, which were determined equal to 14.1 and 20.8% (w/w) of their molecular masses for GOXI and GOXII, respectively. The above difference in the carbohydrate content between the two enzymes seems to influence their pH and thermal stabilities. GOXII proved to be more stable than GOXI at pH values 2.5, 3.0, 8.0, and 9.0. Half-lives of GOXI at pH 3.0 and 8.0 were 8.9 and 17.5 h, respectively, whereas the corresponding values for GOXII were 13.5 and 28.1 h. As far as the thermal stability is concerned, GOXII was also more thermostable than GOXI as judged by the deactivation constants determined at various temperatures. More specifically, the half-lives of GOXI and GOXII, at 45°C, were 12 and 49 h, respectively. These results suggest A. niger BTL probably possesses a secondary glycosylation mechanism that increases the stability of the excreted GOX.
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| 9. |
- 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
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Ingår i: World Journal of Microbiology & Biotechnology. - 0959-3993 .- 1573-0972. ; 17:3, s. 229-234
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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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| 10. |
- Hatzinikolaou, Dimitris G., et al.
(författare)
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Modeling of the simultaneous hydrolysis-ultrafiltration of whey permeate by a thermostable beta-galactosidase from Aspergillus niger
- 2005
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Ingår i: Biochemical engineering journal. - : Elsevier BV. - 1369-703X .- 1873-295X. ; 24:2, s. 161-172
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Tidskriftsartikel (refereegranskat)abstract
- A wild type strain of Aspergillus niger, denoted as BTL, produced elevated levels of β-galactosidase when grown in a low cost medium that contained wheat bran as the sole carbon and energy source. The enzyme was collected, concentrated and partially purified from the culture supernatant. Its kinetic and stability properties were thoroughly examined towards its potential use for the hydrolysis of acid whey permeate lactose. The β-galactosidase of A. niger BTL showed increased pH and thermal stability, with activation energy for the first order deactivation constant equal to 180 kJ/mol at pH 3.5. Lactose hydrolysis by the enzyme was described by Michaelis–Menten kinetics with competitive inhibition only from galactose. An integrated process, concerning the simultaneous hydrolysis–ultrafiltration of whey lactose that incorporated the specific kinetic properties of the β-galactosidase was developed and modeled. The model proved very successful in predicting the behavior of a continuous laboratory hydrolysis–ultrafiltration set up, specifically designed for that purpose. The validated model was finally used in a number of computer simulations in order to investigate the effect of the various process parameters on the overall system performance.
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