期刊
MACROMOLECULAR RESEARCH
卷 16, 期 7, 页码 651-658出版社
POLYMER SOC KOREA
DOI: 10.1007/BF03218575
关键词
lipase PS (R); enzymatic degradation; hydrolysis mechanism; terminal chain; surface adsorption; homopolymer
资金
- Hoseo University [20070094]
- National Research Foundation of Korea [과06B2507] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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 (R), 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.
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