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Please use this identifier to cite or link to this item: http://localhost:8080/xmlui/handle/123456789/1113
Title: Substrate specificities and mechanism of action of multiple alpha-galactosidases from Streptomyces griseoloalbus
Authors: Anisha, G S
Rojan P John
Prema, P
Keywords: Hydrolysis
Hydrolases
Streptomyces griseoloalbus
Natural substrates
H NMR spectroscopy
Retaining mechanism
alpha Galactosidase
Issue Date: 2011
Publisher: Elsevier
Citation: Food Chemistry 124(1):349-353;01 Jan 2011
Abstract: alpha-Galactosidase or melibiase is a versatile enzyme with many potential biotechnological and industrial applications. The substrate specificities of three alpha-galactosidases - alpha-Gal I, alpha-Gal II, and alpha-Gal III - from Streptomyces griseoloalbus were studied using different galactose-containing natural substrates like melibiose, raffinose and stachyose. The kinetic parameters K(m), and V(max) were determined from the Lineweaver-Burk plot. alpha-Gal I showed highest affinity towards melibiose where as alpha-Gal II and alpha-Gal III showed highest affinity towards stachyose. The (1)H NMR studies showed that all the three alpha-galactosidases had a retaining mechanism of hydrolysis.
URI: http://ir.niist.res.in:8080/jspui/handle/123456789/1113
ISSN: 0308-8146
Appears in Collections:2011

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