ePrints@IIScePrints@IISc Home | About | Browse | Latest Additions | Advanced Search | Contact | Help

Lipase specificity for the hydrolysis of poly (vinyl acetate)

Chattopadhyay, Sujay and Sivalingam, G and Madras, Giridhar (2003) Lipase specificity for the hydrolysis of poly (vinyl acetate). In: Polymer Degradation and Stability, 80 (3). pp. 477-483.

[img] PDF
sdarticle3.pdf - Published Version
Restricted to Registered users only

Download (216kB) | Request a copy
Official URL: http://www.sciencedirect.com/science?_ob=ArticleUR...


The effect of lipases on the side chain hydrolysis of poly (vinyl acetate) (PVAc) was investigated in toluene by various lipases, Hog-pancreas (HP), Candida Rugosa (CR), Lipolase-100T (LL), and Novozyme 435 (NV)at 60 degreesC. Gas chromatographs and GC-MS spectra showed the presence of different ester side chains. The different size side chain esters in PVAc get hydrolyzed at different specific rates by the various lipases. Longer side chains are hydrolyzed in the order HP > NV > LL > CR whereas the short chains are hydrolyzed in the reverse order. A continuous distribution kinetics model was proposed that accounts for lipase ndeactivation and determines the rate coefficients ofn hydrolysis of various chain lengths. Lipase deactivation and hydrolysis rate coefficients were determined for each case. The proposed model predicts the experimental data satisfactorily.

Item Type: Journal Article
Publication: Polymer Degradation and Stability
Publisher: Elsevier Science
Additional Information: Copyright of this article belongs to Elsevier Science.
Keywords: Poly (vinyl acetate); Side chain hydrolysis; Lipases; Novozyme;Candida rugosa;Hog pancreas;Lipolase;Lipase deactivation;Continuous distribution kinetics.
Department/Centre: Division of Mechanical Sciences > Chemical Engineering
Date Deposited: 04 Sep 2009 03:34
Last Modified: 19 Sep 2010 04:55
URI: http://eprints.iisc.ac.in/id/eprint/17094

Actions (login required)

View Item View Item