title: [Anomalous temperature dependence of the activity of immobilized alpha-chymotrypsin preparations].
abstract: 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.
authors.forename: L V
authors.initials: LV
authors.lastname: Sigolaeva
authors.forename: N L
authors.initials: NL
authors.lastname: Eremeev
authors.forename: N F
authors.initials: NF
authors.lastname: Kazanskaia
mesh_terms: D000178:Acrylamides; D002384:Catalysis; D002918:Chymotrypsin / Q000378:metabolism*; D004800:Enzymes, Immobilized / Q000378:metabolism*; D007700:Kinetics; D011108:Polymers; D013379:Substrate Specificity; D013696:Temperature; D014867:Water
chemical_list: D000178:Acrylamides; D004800:Enzymes, Immobilized; D011108:Polymers; D014867:Water; D002918:Chymotrypsin
vernacular_title: Anomal'naia temperaturnaia zavisimost' aktivnosti preparatov immobilizovannogo alpha-khimotripsina.