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  • 1
    ISSN: 1432-072X
    Keywords: Candida tropicalis ; alkane utilization ; Yeast peroxisomes ; Long-chain alcohol dehydrogenase ; Long-chain aldehyde dehydrogenase ; Acyl-CoA synthetase ; Glycerol-3-phosphate acyltransferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Long-chain alcohol dehydrogenase and longchain aldehyde dehydrogenase were induced in the cells of Candida tropicalis grown on n-alkanes. Subcellular localization of these dehydrogenases, together with that of acyl-CoA synthetase and glycerol-3-phosphate acyltransferase, was studied in terms of the metabolism of fatty acids derived from n-alkane substrates. Both longchain alcohol and aldehyde dehydrogenases distributed in the fractions of microsomes, mitochondria and peroxisomes obtained from the alkane-grown cells of C. tropicalis. Acyl-CoA synthetase was also located in these three fractions. Glycerol-3-phosphate acyltransferase was found in microsomes and mitochondria, in contrast to fatty acid β-oxidation system localized exclusively in peroxisomes. Similar results of the enzyme localization were also obtained with C. lipolytica grown on n-alkanes. These results suggest strongly that microsomal and mitochondrial dehydrogenases provide long-chain fatty acids to be utilized for lipid synthesis, whereas those in peroxisomes supply fatty acids to be degraded via β-oxidation to yield energy and cell constituents.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A cell suspension in a water-insoluble organic solvent (benzene: n-heptane, 1 : 1 by volume) of Nocardia rhodocrous (previously induced to synthesize steroid Δ1dehydrogenase) rapidly catalyzed the stoichiometric oxidation of 4-androstene-3,17-dione (4-AD) to androst-l,4-diene-3,17-dione (ADD) in the presence of phenazine methosulfate (PMS). High levels of 4-AD or PMS reduced the conversion rates. No appreciable decrease in the conversion rate was observed on adding aqueous buffer solution to the thawed ceils (up to 9.4 g water/g dry cell). The whole cells were immobilized by entrapment in a hydrophilic gel (H-gel) or a lipophilic gel (L-gel) by use of a water-soluble or water-insoluble photocrosslinkable prepolymer. The reticula of H- and L-gel matrices were impregnated with water and organic solvent, respectively. Both the H- and L-gels could convert 4-AD to ADD in the presence of PMS, the L-gel showing a slightly higher conversion rate. Various lines of evidence indicate that the limiting factor is the penetration rate of 4-AD into gel particles for the H-gel, and the penetration rate of PMS for the L-gel. The catalytic activities decreased considerably after several successive runs with the free cell suspension system, while the immobilized cells were more stable, the stability of H-gel and L-gel being almost the same.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 20 (1978), S. 1465-1469 
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 59 (1998), S. 582-586 
    ISSN: 0006-3592
    Keywords: esterase ; genetic recombination ; hydrophobilization ; polyproline ; transesterification reaction ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Polyproline, which is an amphiphilic polypeptide, was incorporated into the carboxyl terminal of an esterase by the recombinant DNA technique. The hydrophobicity of the esterase increased with increasing chain length of polyproline without inducing significant conformational changes. The mutant esterase catalyzed the hydrolysis of long-chain carboxylic acid ester more efficiently than the native esterase. It is considered that the alteration of substrate specificity is due to enhanced access of the mutant esterases to hydrophobic substrates. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:582-586, 1998.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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