The effect of proline insertions on the thermostability of a barley alpha-glucosidase.

doi:10.1093/protein/15.1.29

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Article

The effect of proline insertions on the thermostability of a barley alpha-glucosidase.

Protein engineering - 1 Jan 2002

Muslin E H, Clark S E, Henson C A

Abstract excerpt

The thermal stability of alpha-glucosidase is important because the conversion of starch to fermentable sugars during industrial production of ethanol (e.g. brewing, fuel ethanol production) typically takes place at temperatures of 65-73 degrees C. In this study we investigate the thermostability of alpha-glucosidases from four plant species, compare their deduced amino acid sequences, and test the effect of...

Topics

Amino Acid Sequence
Amino Acid Substitution
Conserved Sequence
Enzyme Stability
Hordeum
Hot Temperature
Molecular Sequence Data
Mutagenesis, Site-Directed
Mutation
Plants
Proline
Protein Structure, Secondary
Recombinant Proteins
Sequence Homology, Amino Acid
alpha-Glucosidases

Source

Open in PubMed

Identifiers

PMID: 11842235
DOI: 10.1093/protein/15.1.29

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