Kinetic investigation of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105 immobilized on oxirane-acrylic beads.

doi:10.1002/jctb.280510205

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Article

Kinetic investigation of penicillin G acylase from a mutant strain of Escherichia coli ATCC 11105 immobilized on oxirane-acrylic beads.

Journal of chemical technology and biotechnology (Oxford, Oxfordshire : 1986) - 1 Jan 1991

Erarslan A, Güray A

Abstract excerpt

Highly purified penicillin G acylase from a mutant derivative of Escherichia coli ATCC 11105 was immobilized on oxirane-acrylic beads by covalent binding via oxirane groups. The highest specific activity, (322 U g-1 dry matrix at 40 degrees C and at pH 8.0) was obtained by using an enzyme solutio...

Topics

Acrylates
Enzyme Stability
Enzymes, Immobilized
Escherichia coli
Ethylene Oxide
Hydrogen-Ion Concentration
Kinetics
Mutation
Penicillanic Acid
Penicillin Amidase
Penicillin G
Thermodynamics

Source

Open in PubMed

Identifiers

PMID: 1369308
DOI: 10.1002/jctb.280510205

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-1369308-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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