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Relationship between Enzyme Adsorption and Enzyme‐Catalyzed Degradation of Polylactides
Author(s) -
Zhao Zhenxian,
Yang Liu,
Hua Jiajie,
Wei Jia,
Gachet Sylvie,
Ghzaoui Abdelslam El,
Li Suming
Publication year - 2008
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.200700180
Subject(s) - adsorption , enzyme , chemistry , molecule , surface tension , degradation (telecommunications) , catalysis , tris , chemical engineering , biophysics , organic chemistry , biochemistry , thermodynamics , telecommunications , physics , biology , computer science , engineering
Abstract The adsorption of proteinase K on PLLA and PDLA films was studied by CA, surface tension, and microscopic measurements. ESEM clearly shows that proteinase K can irreversibly adsorb on PLLA film. In contrast, no enzyme adsorption was detected on PDLA film under the same conditions. The CA of PLLA film rapidly decreases after immersion in Tris buffer containing proteinase K, whereas that of PDLA remains unchanged. These findings indicate that enzyme adsorption may be a prerequisite for enzymatic degradation of polylactide substrates. Surface tension measurements allow calculation of the average area occupied per proteinase K molecule. The results show that the enzyme molecules exhibit a more compact conformation at higher temperature.