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Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the [be...

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the [be...

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_infotracacademiconefile_A468885615

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the [beta]-galactosidase from Bacillus subtilis VTCC-DVN-12-01

About this item

Full title

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the [beta]-galactosidase from Bacillus subtilis VTCC-DVN-12-01

Publisher

BioMed Central Ltd

Journal title

BMC biochemistry, 2016-07, Vol.17 (1)

Language

English

Formats

Publication information

Publisher

BioMed Central Ltd

More information

Scope and Contents

Contents

Background Beta-galactosidase (EC 3.2.1.23), a commercially important enzyme, catalyses the hydrolysis of [beta]-1,3- and [beta]-1,4-galactosyl bonds of polymer or oligosaccharidesas well as transglycosylation of [beta]-galactopyranosides. Due to catalytic properties; [beta]-galactosidase might be useful in the milk industry to hydrolyze lactose an...

Alternative Titles

Full title

Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the [beta]-galactosidase from Bacillus subtilis VTCC-DVN-12-01

Identifiers

Primary Identifiers

Record Identifier

TN_cdi_gale_infotracacademiconefile_A468885615

Permalink

https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_gale_infotracacademiconefile_A468885615

Other Identifiers

ISSN

1471-2091

E-ISSN

1471-2091

DOI

10.1186/s12858-016-0070-0

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