A KINETIC APPROACH TO THE THERMAL INACTIVATION OF AN IMMOBILIZED TRIOSEPHOSPHATE ISOMERASE

被引：3

作者：

ABRAHAM, M

PENZES, Z

SZAJANI, B

机构：

[1] Department of Biochemistry, Attila József University, Szeged, 6701

[2] Institute of Biophysics, Hungarian Academy of Sciences, Szeged

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 1992年 / 40卷 / 04期

关键词：

TRIOSEPHOSPHATE ISOMERASE; IMMOBILIZED; THERMAL STABILITY; KINETIC APPROACH;

D O I：

10.1002/bit.260400411

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：

The process of thermal inactivation of triosephosphate isomerase covalently attached to a silica-based support activated with p-benzoquinone was found to be a complex one. At 50-degrees-C, a characteristic activation preceding the thermal inactivation was observed. Following the intramolecular changes caused by heat, the values of K(M) and v(max) were determined during the activation. It was presumed that the complex thermal inactivation kinetics reflects the microheterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.

引用

页码：525 / 529

页数：5

共 16 条

[1]

ABRAHAM M, 1988, Prikladnaya Biokhimiya i Mikrobiologiya, V24, P499

[2] CHARACTERIZATION AND COMPARISON OF SOLUBLE AND IMMOBILIZED PIG MUSCLE ALDOLASES [J].