Abstract
Poly(butylene succiate) (PBS), poly(butylene succinate-co-L-lactate) (PBSL), and poly(butylene succinate-co-6-hydroxycaproate) (PBSCL) polymers were degraded by lipase PS®, and the enzymatic degradation mechanism of PBS was analyzed in detail. The enzymatic degradation of PBS gave 4-hydroxybutyl succinate (4HBS) as the main product. An exo-type hydrolysis mechanism was proposed based on this observation. The terminal chain of PBS had conformational similarity to ordinary tri- and diglycerides and could be incorporated as a substrate in the active site of this lipase. The surface adsorption of the lipase was much larger on PBS and its copolymer films than on the other polyester films because the lipase adhered quite strongly to the polymer terminal through a specific adsorption mechanism. Kinetic analysis showed that the total number of surface adsorption points per unit area of PBSL and PBSCL copolymers was larger than that of the PBS homopolymer.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
