CATALYTIC ACTIVITY AND DENATURATION OF ENZYMES IN WATER ORGANIC COSOLVENT MIXTURES - ALPHA-CHYMOTRYPSIN AND LACCASE IN MIXED WATER ALCOHOL, WATER GLYCOL AND WATER FORMAMIDE SOLVENTS

Авторы: MOZHAEV VV, KHMELNITSKY YL, SERGEEVA MV, BELOVA AB, KLYACHKO NL, LEVASHOV AV, MARTINEK K.
Журнал: European Journal of Biochemistry
Том: 184
Номер: 3
Год издания: 1989
Первая страница: 597
Последняя страница: 602
DOI: 10.1111/j.1432-1033.1989.tb15055.x
Аннотация: The dependence of the catalytic activities of alpha-chymotrypsin and laccase on the concentration of organic cosolvents (alcohols, glycols and formamides) in mixed aqueous media has a pronounced threshold character: it does not change up to a critical concentration of the non-aqueous cosolvents added, yet further increase of the latter (by only a small percentage, by vol.) leads to an abrupt decrease in enzyme activity. Fluorescence studies indicate that the inactivation results from reversible conformational changes (denaturation) of the enzymes. There is a linear correlation between the critical concentration of residual water (at which the enzyme inactivation occurs in a threshold manner) and the hydrophobicity of the organic cosolvents added. A quantitative criterion is suggested for the selection of organic cosolvents to be used for enzymatic reactions in homogeneous water/organic solvent media.
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