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Enzymatic hydrolysis of poly(D, L-lactide) spread monolayers by cutinase

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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.

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Authors and Affiliations

  1. Biophysical Chemistry Laboratory, University of Sifia, J. Bourchier str. 1, 1126, Sofia, Bulgaria

    T. Z. Ivanova & I. Panaiotov

  2. Pharmacie Galénique, et Biophysique Pharmaceutique Faculté de Pharmacie, 16 Bd Daviers, 49100, Angers, France

    F. Boury & J. E. Proust

  3. ERS 26 “Lypolyse enzymatique” du Centre, National de la Recherche Scientifique, B.P. 71 13402, 9, Marseille, Cedex, France

    R. Verger

Authors
  1. T. Z. Ivanova
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  2. I. Panaiotov
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  3. F. Boury
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  4. J. E. Proust
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  5. R. Verger
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Ivanova, T.Z., Panaiotov, I., Boury, F. et al. Enzymatic hydrolysis of poly(D, L-lactide) spread monolayers by cutinase. Colloid Polym Sci 275, 449–457 (1997). https://doi.org/10.1007/s003960050103

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  • DOI: https://doi.org/10.1007/s003960050103

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