Catalytic properties of glucoamylase immobilized on synthetic carbon material Sibunit

被引:11
作者
Kovalenko, G. A. [1 ]
Perminova, L. V.
Terent'eva, T. G.
Plaksin, G. V.
机构
[1] Russian Acad Sci, Siberian Div, Boreskov Inst Catalysis, Novosibirsk 630090, Russia
[2] Russian Acad Sci, Siberian Div, Inst Hydrocarbon Proc, Omsk 644040, Russia
关键词
Apply Biochemistry; Immobilize Enzyme; Dextrin; Glucoamylase Activity; Mesoporous Carbon Material;
D O I
10.1134/S0003683807040023
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
Glucoamylase (commercial preparation Glucavamorin) was immobilized by sorption on a carbon support Sibunit. Starch saccharification by the resulting biocatalyst (dextrin hydrolysis) was studied. Investigation of the effect of adsorptional immobilization on kinetic parameters of glucoamylase, including the rate constant of thermal inactivation, showed that immobilization of Glucavamorin on Sibunit resulted in a thousand-fold increase in glucoamylase stability in comparison with the dissolved enzyme. Presence of the substrate (dextrins) in the reaction mixture had a considerable stabilizing effect. Increase in dextrin concentration increases the thermostability of the immobilized enzyme. The overall factor of glucoamylase stabilization adsorbed on Sibunit with the presence of 53% dextrin solutions in comparison with the dissolved enzyme approximated 10(5). The biocatalyst for starch saccharification made on the base of Subunit-adsorbed Glucavamorin had a high operational stability. Its half-inactivation time at 60 degrees C exceeded 30 days.
引用
收藏
页码:374 / 378
页数:5
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