Lim Hyun-A, Raku Takao, Tokiwa Yutaka
Institute of Agricultural Science & Technology, Chonbuk National University, Jeonju, 561-756, Korea.
Biotechnol Lett. 2005 Apr;27(7):459-64. doi: 10.1007/s10529-005-2217-8.
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.
使用聚（L-丙交酯）（PLA）、聚（β-羟基丁酸酯）（PHB）、聚（丁二酸乙二酯）（PES）、聚（己二酸乙二酯）（PEA）、聚（丁二酸丁二酯）（PBS）、聚（丁二酸丁二酯-共-己二酸酯）（PBS/A）、聚[低聚（丁二酸丁二酯）-共-（碳酸丁二酯）]（PBS/C）和聚（ε-己内酯）（PCL），研究了α-胰凝乳蛋白酶和其他丝氨酸蛋白酶（胰蛋白酶、弹性蛋白酶、蛋白酶K和枯草杆菌蛋白酶）对各种聚酯水解的底物特异性。α-胰凝乳蛋白酶可以降解PLA和PEA，对PBS/A的活性较低。蛋白酶K和枯草杆菌蛋白酶降解了除PHB以外的几乎所有底物。胰蛋白酶和弹性蛋白酶具有与α-胰凝乳蛋白酶相似的底物特异性。
