A kinetic approach to the thermal inactivation of an immobilized triosephosphate isomerase

M. Abraham, Z. Pénzes, B. Szajáni

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

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 micro-heterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.

Original languageEnglish
Pages (from-to)525-529
Number of pages5
JournalBiotechnology and Bioengineering
Volume40
Issue number4
DOIs
Publication statusPublished - Aug 5 1992

Fingerprint

Triose-Phosphate Isomerase
Hot Temperature
Kinetics
Chemical activation
Enzyme kinetics
Immobilized Enzymes
Silicon Dioxide
Phosphates
Enzymes
Silica
Ions
Molecules
Substrates

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology

Cite this

A kinetic approach to the thermal inactivation of an immobilized triosephosphate isomerase. / Abraham, M.; Pénzes, Z.; Szajáni, B.

In: Biotechnology and Bioengineering, Vol. 40, No. 4, 05.08.1992, p. 525-529.

Research output: Contribution to journalArticle

@article{f2f7dd78d76a4dba85944cd30d015c3c,
title = "A kinetic approach to the thermal inactivation of an immobilized triosephosphate isomerase",
abstract = "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 micro-heterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.",
author = "M. Abraham and Z. P{\'e}nzes and B. Szaj{\'a}ni",
year = "1992",
month = "8",
day = "5",
doi = "10.1002/bit.260400411",
language = "English",
volume = "40",
pages = "525--529",
journal = "Biotechnology and Bioengineering",
issn = "0006-3592",
publisher = "Wiley-VCH Verlag",
number = "4",

}

TY - JOUR

T1 - A kinetic approach to the thermal inactivation of an immobilized triosephosphate isomerase

AU - Abraham, M.

AU - Pénzes, Z.

AU - Szajáni, B.

PY - 1992/8/5

Y1 - 1992/8/5

N2 - 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 micro-heterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.

AB - 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 micro-heterogeneity of the immobilized enzyme molecules. The phosphate ion proved to be a better stabilizer than the substrate.

UR - http://www.scopus.com/inward/record.url?scp=0027112621&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027112621&partnerID=8YFLogxK

U2 - 10.1002/bit.260400411

DO - 10.1002/bit.260400411

M3 - Article

VL - 40

SP - 525

EP - 529

JO - Biotechnology and Bioengineering

JF - Biotechnology and Bioengineering

SN - 0006-3592

IS - 4

ER -