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Lipase specificity for the hydrolysis of poly (vinyl acetate)
S. Chattopadhyay, G. Sivalingam,
Published in
2003
Volume: 80
   
Issue: 3
Pages: 477 - 483
Abstract
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 °C. 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 deactivation and determines the rate coefficients of hydrolysis of various chain lengths. Lipase deactivation and hydrolysis rate coefficients were determined for each case. The proposed model predicts the experimental data satisfactorily. © 2003 Elsevier Science Ltd. All rights reserved.
About the journal
JournalPolymer Degradation and Stability
ISSN01413910