Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency.

doi:10.1007/s12010-009-8879-2

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Article

Engineering of a Bacillus alpha-amylase with improved thermostability and calcium independency.

Applied biochemistry and biotechnology - 1 Sept 2010

Ghollasi Marzieh, Khajeh Khosro, Naderi-Manesh Hossein, Ghasemi Atiyeh

Abstract excerpt

Successful industrial use of amylases requires that they are sufficiently stable and active at application conditions, e.g., at high temperature in starch-liquefaction process. In the present study, site-directed mutagenesis was used to enhance the thermal stability and calcium independency of a mesophilic alpha-amylase from Bacillus megaterium WHO. Mutations (A53S and H58I) were designed at the calcium-binding...

Topics

Amino Acid Sequence
Bacillus megaterium
Calcium
Cloning, Molecular
Entropy
Enzyme Stability
Kinetics
Molecular Sequence Data
Mutation
Protein Structure, Secondary
Recombinant Proteins
Sequence Alignment
Temperature
Unfolded Protein Response
alpha-Amylases

Source

Open in PubMed

Identifiers

PMID: 20177823
DOI: 10.1007/s12010-009-8879-2

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