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  • 1
    Electronic Resource
    Electronic Resource
    Purification and some properties of the mannanases fromThielavia terrestris (1990)
    Springer
    Journal of industrial microbiology and biotechnology 6 (1990), S. 269-274 
    Details
    ISSN: 1476-5535
    Keywords: Thielavia terrestris ; Mannanase ; Mannosidase ; Hemicellulase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary Thielavia terrestris NRRL 8126 cell free supernatants contained mannanase and β-mannosidase when cultured on a complex media containing locust bean gum. Using acetone precipitation, SP-Sephadex C50 ion exchange chromatography and preparative gel electrophoresis, the crude enzyme was resolved into one β-d-mannosidase and four β-d-mannanase components. β-d-mannosidase had a specific activity of 0.02 (U/mg) onp-nitrophenyl-β-d-mannopyranoside substrate. Mannanase components M1, M2, M3 and M4 had specific activities of 28.2, 38.7, 52.8 and 4.17 (U/mg) respectively on purified locust bean galactomannan substrate. pH optima for the enzymes were in the range 4.5–5.5. Mannanase component M4 manifested the greatest thermostability, retaining full activity for 3 h at 60°C. Molecular weights determined by SDS-PAGE were 72 000 for β-mannosidase and 52 000, 30 000, 55 000 and 89 000 for M1, M2, M3 and M4 respectively. Carbohydrate contents of the enzymes ranged from 6–36%. Preliminary studies indicate that enzyme components hydrolyse the mannan substrate in a synergistic manner.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01575872
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  • 2
    Electronic Resource
    Electronic Resource
    Production of docosahexaenoic acid byThraustochytrium roseum (1994)
    Springer
    Journal of industrial microbiology and biotechnology 13 (1994), S. 238-241 
    Details
    ISSN: 1476-5535
    Keywords: Docosahexaenoic acid ; Thraustochytrium, Omega-3 fatty acids ; Fermentation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Summary When threeThraustochytrium stains were cultivated in liquid media containing 2.5% starch and 0.2% yeast extract, initial pH 6.0, with shaking under fluorescent light for five days at 25°C, similar biomass yields were observed (9.7–10.3 g L−1). Contents of docosahexaenoic acid (DHA) in biomass varied: 0.15, 3.55 and 6.40% w/w forT. striatum ATCC 24473,T. aureum ATCC 34304 andT. roseum ATCC 28210, respectively. In further studies,T. roseum produced a maximum titer of 0.85 g of DHA per liter of culture broth. The DHA content of total lipids ranged from 46–49% w/w.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01569755
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  • 3
    Electronic Resource
    Electronic Resource
    Studies of the reductive biotransformation of selected carbonyl compounds by whole cells and extracts of baker's yeast, Saccharomyces carevisiae (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 1280-1284 
    Details
    ISSN: 0006-3592
    Keywords: Saccharomyces cerevisiae ; biotransformation ; oxidoreductases ; carbonyl ; stereospecific ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The progress of reductive biotransformations of a variety of earbonyl compounds by whole cells of baker's yeast was monitored with time. Biotransformations rates ranged from 0.11 to 112.12 mg product formed per g dry yeast per h. While rapid biotransformations of citronellal and ethyl benzoylformate were observed, complete conversion of substrate to product did not occur. Reductive conversions of ethyl- and methyl-acetoacetate went to completion in 6 and 12 h respectively. Ethyl mandelate was produced stereoselectively, favoring the (R)- stereoisomer and ethyl and methyl-3-hydroxybutyrate were produced with (S)-enantiospecificity. Yeast crude extract and resuspended presence of NAD(P)H. Ethyl benzoylformate and methyl-and ethyl-acetoacetate were preferentially reduced by yeast crude extract as compared to resuspended pellet and, in the case of the former two substrates, the reaction manifested a preference for NADPH over NADH.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260381104
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  • 4
    Electronic Resource
    Electronic Resource
    Reductive biotransformations of organic compounds by saccharomyces cerevisiae: Study of oxidoreductases involved using electrophoretic zymograms (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 457-461 
    Details
    ISSN: 0006-3592
    Keywords: Saccharomyces cerevisiae ; biotransformations ; zymograms ; carbonyl reduction ; baker's yeast ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The role of oxidoreductases in reduction of carbonyl compounds was investigated by application of zymogram techniques. Eight bands were observed using ethanol with nicotinamide adenine dinucleotide (NAD) as coenzyme. Bands observed with lactic acid and (R)-(-)-phenyl-1,2-ethanediol with nicotinamide adenine dinucleotide phosphate (NADP) had similar Rm values. 2-Hydroxyvalerate and malate manifested bands having similar Rm values and were active with both NAD and NADP. Based on their structural similarity and identical Rm values, oxidation of 1,4-cyclooctanediol (band #2) and cis-1,5-cyclooctanediol may be due to a common enzyme. The PAGE-zymogram technique may be used on a preparative scale to facilitate purification and full characterization on the observed stained bands.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390413
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  • 5
    Electronic Resource
    Electronic Resource
    Reductive biotransformation by wild type and mutant strains of Saccharomyces cerevisiae in aqueous-organic solvent biphasic systems (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 870-876 
    Details
    ISSN: 0006-3592
    Keywords: Saccharomyces cerevisiae ; benzyl alcohol ; reductive biotransformation ; biphasic systems ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Whole cells of Saccharomyces cerevisiae analyzed the conversion of benzaldehyde to benzyl alcohol in aqueous-organic biphasic media. Reaction rate increased dramatically as moisture content of the solvent was increased in the range 0% to 2%. The highest biotransformation rates were observed when hexane was used as organic solvent. Benzaldehyde was also converted to benzyl alcohol by a cell-free crude extract in biphasic systems containing hexane, although the rate of product formation was much lower. Mutant strains of S. cerevisiae lacking some or all of the ADH isoenzymes, ADH I, II, and III, manifested similar rates for bioconversion of benzaldehyde to benzyl alcohol in both aqueous and two-phase systems. In general, conversion rates observed in aqueous media were 2 to 3 times higher than those observed in hexane containing 2% moisture.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260390809
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  • 6
    Electronic Resource
    Electronic Resource
    Factors affecting 2-hydroxypropiophenone formation by benzoylformate decarboxylase from Pseudomonas putida (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 39 (1992), S. 1058-1063 
    Details
    ISSN: 0006-3592
    Keywords: 2-hydroxypropiophenone ; Pseudomonas putida ; benzoylformate decarboxylase ; biotransformation ; acyloin ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Benzoylformate (100 mM) was quantitatively converted to the acyloin compound, 2-hydroxypropiophenone (61.76 mM) and benzaldehyde (38.2 mM) by an enzyme extract from Pseudomonas putida ATCC 12633 in the presence of 1.6M acetaldehyde. Biotransformations were carried out at pH 6.0 and 30°C with an incubation time of 60 min. Activity of the acyloin forming enzyme, benzoylformate decarboxylase, was 1.23 units/mL in the biotransformation mixture. Acyloin formation increased dramatically with pH in the range 4-5 and had a broad activity plateau in the pH range 5-8. A broad temperature optimum for acyloin formation was also observed in the range 20-40°C.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260391010
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  • 7
    Electronic Resource
    Electronic Resource
    Production of L-phenylacetyl carbinol by biotransformation: Product and by-product formation and activities of the key enzymes in wild-type and ADH isoenzyme mutants of Saccharomyces cerevisiae (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 493-498 
    Details
    ISSN: 0006-3592
    Keywords: L-phenylacetyl carbinol ; ADH isoenzymes ; ethanol ; benzyl alcohol ; Saccharomyces cerevisiae ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: The capacities of yeast wild-type and mutants strains known to lack specific ADH isoenzymes to produce L-phenylacetyl carbinol (PAC) and benzyl alcohol in biotransformation trials were also investigated. Pyruvate decarboxylase activity, responsible for PAC formation and ADH activity, which can participate in reduction of benzaldehyde to benzyl alcohol, was also determined in each strain. In addition, the capacity of each strain to produce ethanol was investigated. Mutant strains lacking all of the isoenzymes, ADH-I, ADH-II, and ADH-III, still exhibited some ADH activity and were capable of production of benzyl alcohol and ethanol.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380507
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  • 8
    Electronic Resource
    Electronic Resource
    Application of lipase to concentrate the docosahexaenoic acid (DHA) fraction of fish oil (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 38 (1991), S. 956-959 
    Details
    ISSN: 0006-3592
    Keywords: Rhizopus niveus ; DHA ; omega-3 fatty acid ; specification ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A commercial lipase preparation from Rhizopus niveus was used to concentrate the omega-3 fatty acid, docosahexaenoic acid (DHA) component in fish oil. The DHA content of cod-liver oil was 9.64% (w/w) of total fatty acids. Enzymatic digestion conditions were established which produced a DHA content in the monoglycerides fraction of 29.17% (w/w) of total fatty acid, triglyceride, and diglyceride components were 5.72, 9.95, and 15316%, respectively.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260380818
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  • 9
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    Lipase-catalyzed esterification of glycerol and n-3 polyunsaturated fatty acid concentrate in organic solvent (1993)
    Wiley
    Details
    Publication Date: 1993-08-01
    Print ISSN: 0003-021X
    Electronic ISSN: 1558-9331
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Wiley
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  • 10
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    Effects of agingmortierellamycelium on production of arachidonic and eicosapentaenoic acids (1991)
    Wiley
    Details
    Publication Date: 1991-10-01
    Print ISSN: 0003-021X
    Electronic ISSN: 1558-9331
    Topics: Chemistry and Pharmacology , Process Engineering, Biotechnology, Nutrition Technology
    Published by Wiley
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