Hydrolysis of polyesters by serine proteases

被引：77

作者：

Lim, HA

Raku, T

Tokiwa, Y

机构：

[1] Natl Inst Adv Ind Sci & Technol, Tsukuba, Ibaraki 3058566, Japan

[2] Chonbuk Natl Univ, Inst Agr Sci & Technol, Jeonju 561756, South Korea

来源：

BIOTECHNOLOGY LETTERS | 2005年 / 27卷 / 07期

关键词：

biodegradable; alpha-chymotrypsin; polyesters; poly(L-lactide); serine proteases;

D O I：

10.1007/s10529-005-2217-8

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The substrate specificity of alpha-chymotrypsin and other serine proteases, trypsin, elastase, proteinase K and subtilisin, towards hydrolysis of various polyesters was examined using poly(L-lactide) (PLA), poly(beta-hydroxybutyrate) (PHB), poly(ethylene succinate) (PES), poly(ethylene adipate) (PEA), poly(butylene succinate) (PBS), poly(butylene succinate-co-adipate) (PBS/A), poly[oligo(tetramethylene succinate)-co-(tetramethylane carbonate)] (PBS/C), and poly(epsilon-caprolactone) (PCL). alpha-Chymotrypsin could degrade PLA and PEA with a lower activity on PBS/A. Proteinase K and subtilisin degraded almost all substrates other than PHB. Trypsin and elastase had similar substrate specificities to alpha-chymotrypsin.

引用

收藏

页码：459 / 464

页数：6

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