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Copolyesteramides, 10. Enzymatic degradation of 6‐iminohexanoyl/12‐oxydodecanoyl copolyesteramides
Author(s) -
Goodman Isaac,
Rodríguez Maria Teresa
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(19990101)200:1<44::aid-macp44>3.0.co;2-1
Subject(s) - amide , polyester , chymotrypsin , chemistry , hydrolysis , polymer chemistry , copolymer , collagenase , substrate (aquarium) , degradation (telecommunications) , protease , enzyme , peptide bond , nylon 6 , polymer , cleavage (geology) , trypsin , organic chemistry , materials science , composite material , telecommunications , oceanography , fracture (geology) , computer science , geology
Films of several 6‐iminohexanoyl/12‐oxydodecanoyl random copolymers containing from 19 to 46 wt.‐% (29–60 mol‐%) of 6‐iminohexanoyl units, together with comparison films of nylon 6 homopolymer, were incubated at pH 7,4 in vitro for 336 h at 37° with solutions of protease, collagenase, α‐chymotrypsin and pancreatin. The first three mentioned enzymes were without visible effect upon any of the polymer films, and there was no significant evidence with any enzyme or substrate of the formation of 6‐aminohexanoic acid as a product of amide‐bond splitting. By contrast, incubation with pancreatin caused the topochemical surface erosion of each copolyesteramide (but not of nylon 6), with the depletion of ester group content in the surface layer and the development of an amide‐richer characteristic striated surface morphology. Random incorporation of amide groups into polyesters, in the form of oligoamide sequences, is suggested as a means of protecting the ester component against esterolytic attack.