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  • 1
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Notes: 2 H). As a consequence, the former proteolytic enzyme gained peroxidase activity and catalyzed the selective reduction of hydroperoxides. Due to the identical binding sites of the semisynthetic peroxidase and the protease, the substrate selectivity of seleno-subtilisin was predictable in view of the well-known selectivity of subtilisin.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 59 (1998), S. 786-791 
    ISSN: 0006-3592
    Keywords: seleno-subtilisin ; subtilisin ; semisynthetic enzyme ; peroxidase ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: A simplified and up-scaled synthesis of the semisynthetic peroxidase seleno-subtilisin was developed. Highly purified to technical grade subtilisin preparations from Bacillus licheniformis and Bacillus amyloliquefaciens were applied as starting materials. Activation of Ser 221 with phenylmethanesulfonyl fluoride, nucleophilic substitution by sodium hydrogen selenide, and oxidation to the seleninic acid with hydrogen peroxide completed the chemical active-site modification. The reactions were accomplished with a minimum of simple work-up procedures in 10 g scale. Kinetics and enantioselectivity of the preparations were tested using 1-phenylethyl hydroperoxide. For the first time, an up-scaled synthesis of a semisynthetic enzyme is available. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 59:786-791, 1998.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Journal of High Resolution Chromatography 20 (1997), S. 351-354 
    ISSN: 0935-6304
    Keywords: MDGC ; MCSS ; α-Ketol ; Sherry ; Solerone ; Biogenesis ; Chemistry ; Analytical Chemistry and Spectroscopy
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The enantiomeric distrubution of solerone (5-oxo-4-hexanolide) 1, ethyl 4-hydroxy- 5-oxohexanoate 2, ethyl 5-hydroxy-4-oxohexanoate 3, 4-oxo-5-hexanolide 4, and solerol (5-hydroxy-4-hexanolide) 5 in sherry wines was determined by several HRGC techniques. While gas chromatography-mass spectrometry on chiral cyclodextrin phases (chiral GC-MS) prevented any racemization of α-ketols 2 and 3 caused by keto-enol tautomerization during analysis, multidimensional gas chromatography MDGC (coupled either by “live-T” switching or by “moving column stream switching” MCSS) led to rearranged constitutional-and stereoisomers. The stereochemical results are discussed regarding the biogenesis of sherry constituents 1-5.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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