Immobilization of pig muscle aldolase on a silica-based support

L. Horváth, Magdolna Ábrahám, L. Boross, B. Szajáni

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2 Citations (Scopus)

Abstract

Pig muscle aldolase was covalently attached to a silica-based support possessing aldehyde functional groups. The activity of the immobilized enzyme was 37 U/g solid, and the specific activity calculated on a bound protein basis was 1.9 U/mg protein. The optimum pH for the catalytic activity was pH 7.5. The apparent optimum temperature was found to be 45°C. The Km app value of the immobilized aldolase with D-fructose 1,6-diphosphate as substrate was 1.25 ×10-4 M. The conformational stability was improved by the immobilization. The immobilized aldolase was used for the continuous splitting of D-fructose 1,6-diphosphate.

Original languageEnglish
Pages (from-to)223-235
Number of pages13
JournalApplied Biochemistry and Biotechnology
Volume22
Issue number3
DOIs
Publication statusPublished - Dec 1 1989

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Keywords

  • Aldolase, immobilized
  • D-fructose 1,6-diphosphate splitting
  • catalytic properties, immobilized aldolase
  • enzyme reactor
  • pig muscle aldolase
  • stability tests, immobilized aldolase
  • support, silica-based

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology

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