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Article

Activity and thermal stability of genetically truncated forms of Aspergillus glucoamylase.

Gene - 2 Jul 1990

Evans R, Ford C, Sierks M, Nikolov Z, Svensson B

Abstract excerpt

Glucoamylase (GA) from Aspergillus awamori (EC 3.2.1.3) is a secreted starch hydrolase with a large catalytic domain (aa 1-440), a starch-binding domain (aa 513-616), and a highly O-glycosylated region of 72 aa of unknown function that links the catalytic and starch-binding domains. We have genet...

Topics

Amino Acid Sequence
Aspergillus
Base Sequence
Enzyme Stability
Genetic Vectors
Glucan 1,4-alpha-Glucosidase
Glycosylation
Kinetics
Molecular Sequence Data
Mutation
Plasmids
Thermodynamics

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Identifiers

PMID: 2119327
DOI: 10.1016/0378-1119(90)90174-p

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-2119327-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

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

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