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/2074/1166

Full metadata record

DC FieldValueLanguage
dc.contributor.authorRoy, Ipsita-
dc.contributor.authorSardar, Meryam-
dc.contributor.authorGupta, Munishwar N-
dc.date.accessioned2006-01-18T03:45:57Z-
dc.date.available2006-01-18T03:45:57Z-
dc.date.issued2003-
dc.identifier.citationEnzyme and Microbial Technology, 32(5), 582-588en
dc.identifier.urihttp://eprint.iitd.ac.in/dspace/handle/2074/1166-
dc.description.abstractIt has been shown that a commercially available pectinase, Pectinex™, hydrolyzes chitin fairly efficiently with a Km of 2.2 mg ml−1 of chitin and Vmax equal to 6.5 nmol min−1 mg−1. The pH optimum range (5.0–6.0) and temperature optimum range (55–65 °C) for this unusual activity are more in agreement with the corresponding known values for chitinases rather than the values observed in case of its pectinase activity. The half lives (of chitinolytic activity) of 81 and 76 min at 55 and 65 °C indicate that the chitinolytic activity survives much better that the pectinase activity of the molecule. The occurrence of a carboxyl group in both pectinases and chitinases suggests that similar active site designs may be responsible for this unusual and useful activity of Pectinex™.en
dc.format.extent520891 bytes-
dc.format.mimetypeapplication/pdf-
dc.language.isoenen
dc.subjectBiomass conversionen
dc.subjectChitinaseen
dc.subjectChitin hydrolysisen
dc.subjectPectinaseen
dc.subjectPectinex™en
dc.titleHydrolysis of chitin by Pectinex™en
dc.typeArticleen
Appears in Collections:Chemistry

Files in This Item:

File Description SizeFormat
royhyd2003.pdf508.68 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