NDLI: Enzyme Modification by Natural Chemical Chaperons of Microorganisms

Content Provider	Springer Nature Link
Author	Martirosova, E. I. Karpekina, T. A. El' Registan, G. I.
Copyright Year	2004
Abstract	We demonstrated for the first time that alkyl hydroxybenzenes (the d$_{1}$ microbial autoregulatory factors involved in stress responses of cells) are capable of stabilizing enzymes in aqueous media and increasing their catalytic activity. The stabilizing effect of a chemical analogue of alkyl hydroxybenzenes, C$_{7}$-AHB, was established in in vitro studies with enzymes of microbial origin: a protease produced by Bacillus licheniformis, cellulase produced by Trichoderma viride, and α-amylase produced by Bacillus subtilis. This effect manifested itself in considerable extension of the temperature and pH ranges of the enzymatic activity. The modulation of the catalytic activities of the stabilized enzymes depended on the C$_{7}$-AHB concentration and on the time of preincubation of the complexes obtained. We demonstrated that not only enzymes but also their polymeric substrates formed complexes with C$_{7}$-AHB and this significantly influenced the efficiency of hydrolytic reactions. We also conducted comparative studies on the efficiency of hydrolytic reactions in systems in which the structure of enzymes and/or substrates was modified with C$_{7}$-AHB.
Starting Page	609
Ending Page	615
Page Count	7
File Format	PDF
ISSN	00262617
Journal	Microbiology
Volume Number	73
Issue Number	5
e-ISSN	16083237
Language	English
Publisher	Kluwer Academic Publishers-Plenum Publishers
Publisher Date	2004-01-01
Publisher Place	New York
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Medical Microbiology Microbiology
Content Type	Text
Resource Type	Article
Subject	Microbiology Applied Microbiology and Biotechnology

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