DSpace
 

EPrints@IIT Delhi >
Faculty Research Publicatons  >
Chemistry >

Please use this identifier to cite or link to this item: http://eprint.iitd.ac.in/handle/2074/2333

Full metadata record

DC FieldValueLanguage
dc.contributor.authorAgarwal, Ritu-
dc.contributor.authorGupta, M N-
dc.date.accessioned2006-12-06T06:35:38Z-
dc.date.available2006-12-06T06:35:38Z-
dc.date.issued1994-
dc.identifier.citationBioresource Technology, 49(3), 223-225p.en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/2333-
dc.description.abstractIt was found that Concanavalin A (Con A) accelerates the rates of hydrolysis of E. coli beta-galactosidase and yeast invertase by binding to the product (glucose) formed in the reaction. The effect of Con A can be made more significant by adding fresh Con A, as the initially added Con A becomes saturated. In this fashion, 38% of sucrose could be hydrolysed in the presence of Con A, instead of 22% hydrolysis observed without the presence of lectin.en
dc.format.extent108039 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectCon Aen
dc.subjectbeta-galactosidaseen
dc.subjectinvertaseen
dc.subjectlactose hydrolysisen
dc.subjectsucrose hydrolysisen
dc.titleEffect of presence of concanavalin a on enzymatic hydrolysis of lactose and sucroseen
dc.typeArticleen
Appears in Collections:Chemistry

Files in This Item:

File Description SizeFormat
agarwaleff94.pdf105.51 kBAdobe PDFView/Open
View Statistics

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Valid XHTML 1.0! DSpace Software Copyright © 2002-2010  Duraspace - Feedback