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Article

Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase.

Protein engineering - 1 Aug 1998

Li Y, Coutinho P M, Ford C

Abstract excerpt

Two additional disulfide bonds and three combined thermostabilizing mutations were introduced into Aspergillus awamori glucoamylase to test their effects on enzyme thermostability and catalytic properties. The single cysteine mutations N20C, A27C, T72C and A471C were made and combined to produce the double cysteine mutations N20C/ A27C and T72C/A471C. The double cysteine mutants were expressed efficiently in...

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Identifiers

PMID: 9749918
DOI: 10.1093/protein/11.8.661

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Effect on thermostability and catalytic activity of introducing disulfide bonds into Aspergillus awamori glucoamylase.PMID 9749918Read ↗

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