Immobilized triosephosphate isomerases. A comparative study.

M. Abrahám, A. Alexin, B. Szajáni

Research output: Contribution to journalArticle

1 Citation (Scopus)

Abstract

Pig muscle triosephosphate isomerase was covalently attached to polyacrylamide and silica-based supports possessing carboxylic or aldehyde functional groups or activated with p-benzoquinone. A silica-based support activated with p-benzoquinone proved to be the most advantageous. There were no profound alterations in the catalytic properties as a result of the immobilization. The immobilization enhanced the resistance against urea and heat treatment. At the start of the treatments, the enzyme was activated. The extent of activation depended on the pH, and on the buffer and salt concentrations. Increase of the ionic strength decreased or eliminated the activation. The phosphate ion had a specific effect on the thermal inactivation.

Original languageEnglish
Pages (from-to)1-12
Number of pages12
JournalApplied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology
Volume36
Issue number1
Publication statusPublished - Jul 1992

Fingerprint

Triose-Phosphate Isomerase
Silicon Dioxide
Immobilization
Hot Temperature
Chemical activation
Silica
Polyacrylates
Ionic strength
Aldehydes
Urea
Osmolar Concentration
Functional groups
Muscle
Buffers
Phosphates
Swine
Enzymes
Salts
Heat treatment
Ions

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Biotechnology
  • Bioengineering

Cite this

Immobilized triosephosphate isomerases. A comparative study. / Abrahám, M.; Alexin, A.; Szajáni, B.

In: Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology, Vol. 36, No. 1, 07.1992, p. 1-12.

Research output: Contribution to journalArticle

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