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Substrate specificities and mechanism of action of multiple alpha-galactosidases from Streptomyces griseoloalbus
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| dc.contributor.author | Anisha, G S | |
| dc.contributor.author | Rojan P John | |
| dc.contributor.author | Prema, P | |
| dc.date.accessioned | 2014-01-22T09:06:59Z | |
| dc.date.available | 2014-01-22T09:06:59Z | |
| dc.date.issued | 2011 | |
| dc.identifier.citation | Food Chemistry 124(1):349-353;01 Jan 2011 | en_US |
| dc.identifier.issn | 0308-8146 | |
| dc.identifier.uri | http://ir.niist.res.in:8080/jspui/handle/123456789/1113 | |
| dc.description.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. | en_US |
| dc.language.iso | en | en_US |
| dc.publisher | Elsevier | en_US |
| dc.subject | Hydrolysis | en_US |
| dc.subject | Hydrolases | en_US |
| dc.subject | Streptomyces griseoloalbus | en_US |
| dc.subject | Natural substrates | en_US |
| dc.subject | H NMR spectroscopy | en_US |
| dc.subject | Retaining mechanism | en_US |
| dc.subject | alpha Galactosidase | en_US |
| dc.title | Substrate specificities and mechanism of action of multiple alpha-galactosidases from Streptomyces griseoloalbus | en_US |
| dc.type | Article | en_US |
