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Catalytic activity of alpha-chymotrypsin preparations covalently included in the matrix of the poly-N-isopropylacrylamide gel does not follow Arrhenius equation above the low critical temperature of the polymer dissolution. Starting from this temperature, at which the changes of polymer structure takes place (hydrophobization), the temperature increase results in a rate lowering for the chemical reaction catalyzed by the enzyme. This phenomenon is reversible. A correlation between temperature dependence of the immobilized alpha-chymotrypsin activity and the dehydration degree of the carrier is observed. The decrease of the water content in the matrix causes a change of the substrate specificity of the immobilized alpha-chymotrypsin.
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
April 1971,
Biochemistry,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
March 1981,
Biochemistry,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
April 1976,
Biochemistry,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
September 1984,
Biotechnology and bioengineering,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
August 1982,
Journal of biochemistry,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
September 1993,
The Journal of biological chemistry,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
April 1985,
Physical review. B, Condensed matter,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
January 1977,
Advances in experimental medicine and biology,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
January 1987,
Methods in enzymology,
L V Sigolaeva, and
N L Eremeev, and
N F Kazanskaia
August 1971,
Angewandte Chemie (International ed. in English),
