Abstract
We demonstrated for the first time that alkyl hydroxybenzenes (the d1 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, C7-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 C7-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 C7-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 C7-AHB.
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Martirosova, E.I., Karpekina, T.A. & El'-Registan, G.I. Enzyme Modification by Natural Chemical Chaperons of Microorganisms. Microbiology 73, 609–615 (2004). https://doi.org/10.1023/B:MICI.0000044252.10568.08
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DOI: https://doi.org/10.1023/B:MICI.0000044252.10568.08