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dc.contributor.authorAnisha, G S-
dc.contributor.authorRojan P John-
dc.contributor.authorPrema, P-
dc.date.accessioned2014-01-22T09:06:59Z-
dc.date.available2014-01-22T09:06:59Z-
dc.date.issued2011-
dc.identifier.citationFood Chemistry 124(1):349-353;01 Jan 2011en_US
dc.identifier.issn0308-8146-
dc.identifier.urihttp://ir.niist.res.in:8080/jspui/handle/123456789/1113-
dc.description.abstractalpha-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.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.subjectHydrolysisen_US
dc.subjectHydrolasesen_US
dc.subjectStreptomyces griseoloalbusen_US
dc.subjectNatural substratesen_US
dc.subjectH NMR spectroscopyen_US
dc.subjectRetaining mechanismen_US
dc.subjectalpha Galactosidaseen_US
dc.titleSubstrate specificities and mechanism of action of multiple alpha-galactosidases from Streptomyces griseoloalbusen_US
dc.typeArticleen_US
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