Enzymatic hydrolysis of poly(D, L-lactide) spread monolayers by cutinase |
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| Authors: | T. Z. Ivanova I. Panaiotov F. Boury J. E. Proust R. Verger |
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| Affiliation: | (1) Biophysical Chemistry Laboratory University of Sifia J. Bourchier str. 1 1126 Sofia, Bulgaria, BG;(2) Pharmacie Galénique et Biophysique Pharmaceutique Faculté de Pharmacie 16 Bd Daviers 49100 Angers, France, FR;(3) ERS 26 “Lypolyse enzymatique” du Centre National de la Recherche Scientifique B.P. 71 13402 Marseille Cedex 9, France, FR |
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| Abstract: | ![]()
The enzymatic hydrolysis of a model poly(D,L-lactide) by cutinase was studied by using a barostat surface balance. A theoretical approach based on the adaptation of the Michaelis–Menten scheme at the interface and a process of random fragmentation of the macromolecules was developed. The role of the interfacial organisation of the reaction products was discussed. Hydrolysis rate constant values and the specific activity were estimated and compared with those obtained for the hydrolysis of lipid monolayers. The process of fragmentation of the interfacial polymer structures was visualised by using AFM imaging. Received: 19 August 1996 Accepted: 13 December 1996 |
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| Keywords: | Poly(D L-lactide) spread monolayer enzymatic hydrolysis cutinase |
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