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Synthesis and enzymatic degradation of poly(ester‐amide) stereocopolymers derived from alanine
Author(s) -
Nagata Minoru
Publication year - 1999
Publication title -
macromolecular chemistry and physics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.57
H-Index - 112
eISSN - 1521-3935
pISSN - 1022-1352
DOI - 10.1002/(sici)1521-3935(19990901)200:9<2059::aid-macp2059>3.0.co;2-n
Subject(s) - papain , chemistry , polyamide , hydrolysis , amide , lipase , chymotrypsin , enzyme , proteolytic enzymes , polymer chemistry , alanine , enzymatic hydrolysis , organic chemistry , trypsin , amino acid , biochemistry
Poly(ester‐amide)s with L ‐alanine contents of 100 (LalaS‐100), 90, 80, 70, 50, 30 and 0 were prepared by interfacial polycondensation of the mixture of 1,6‐hexanediol diester of L ‐ and D ‐alanine with sebacoyl chloride. The enzymatic degradation of the poly(ester‐amide)s was followed by the weight loss in a buffer solution (pH 7.2) of proteolytic enzymes (proteinase‐K, papain and α ‐chymotrypsin) and lipase enzymes ( R. delemar, P. cepacia and C. rugosa ) at 37°C. The former enzymes degrade LalaS‐100 much faster than the latter. Above all proteinase‐K degrades it most rapidly and the weight loss is about 78% after 8 h of incubation. It was found that the degradation with the proteolytic enzymes is not caused by hydrolysis of the semi‐peptide linkage but of the ester linkage. The effect of the stereochemical composition on the enzymatic degradation was examined using proteinase‐K and papain, which degrades LalaS‐100 (100% L ) as opposed to LalaS‐0 (100% D ). In contrast, the highest rate of degradation was observed for LalaS‐90.