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. 1990 Nov;56(11):3612–3614. doi: 10.1128/aem.56.11.3612-3614.1990

Does single-amino-acid replacement work in favor of or against improvement of the thermostability of immobilized enzyme?

J Koizumi 1, M Zhang 1, T Imanaka 1, S Aiba 1
PMCID: PMC185035  PMID: 2176451

Abstract

Thermostabilities of kanamycin nucleotidyltransferase and of its mutants that became thermostable, in the free state, because of single-amino-acid replacements were studied after immobilization of the enzymes on cyanogen bromide-activated Sephadex G-200 particles. Lys in place of Gln at position 102 decreased the thermostability of the immobilized enzyme, whereas replacement with other amino acids enhanced it.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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