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A kinetic approach to the thermal inactivation of an imobilized triosephosphate isomerase
Author(s) -
Ábrahám Magdolna,
Pénzes Zsolt,
Szajáani Béla
Publication year - 1992
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.260400411
Subject(s) - triosephosphate isomerase , kinetic energy , chemistry , isomerase , biochemistry , enzyme , physics , quantum mechanics
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°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. © 1992 John Wiley & Sons, Inc.