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| 2. |
- Katapodis, Petros, et al.
(författare)
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Production of β-Fructofuranosidase from Sporotrichum thermophile and Its Application in the Synthesis of Fructooligosaccharides
- 2003
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Ingår i: Food biotechnology. - 0890-5436 .- 1532-4249. ; 17:1, s. 1-14
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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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| 3. |
- 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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| 4. |
- Mamma, Diomi, et al.
(författare)
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Biodegradation of phenol by acclimatized Pseudomonas putida cells using glucose as an added growth substrate
- 2004
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Ingår i: Journal of Environmental Science and Health. Part A. - 1093-4529 .- 1532-4117. ; 39:8, s. 2093-2104
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Tidskriftsartikel (refereegranskat)abstract
- Biodegradation of phenol, a pollutant derived from many industrial processes, was achieved through acclimatized Pseudomonas putida cells. The strategy to overcome the inhibitory effect of phenol on microbial growth involved the addition of glucose, a conventional carbon source. A factorial experimental design was employed in order to optimize the initial phenol and glucose concentrations. The optimum conditions found were applied in 2-lt bioreactors. The development of acclimatized cells and the use of glucose as an added growth substrate resulted in a significant phenol degradation rate of 60.7 mg L−1 h−1 with a complete removal of 1200 mg L−1 phenol.
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