Szewczuk A, Ziomek E, Mordarski M, Siewiński M, Wieczorek J
Biotechnol Bioeng. 1979 Sep;21(9):1543-52. doi: 10.1002/bit.260210904.
An enzyme preparation in a spherical granule form was obtained by copolymerization of penicillin amidase (EC 3.5.1.11) (previously modified with maleic anhydride) and acrylamide via a crosslinking agent. As compared with the native enzyme, immobilized amidase is more resistant to heating, has a lower affinity to benzylpenicillin, and is less inhibited by phenylacetate. Its substrate specificity and optimum pH remain unchanged.
通过青霉素酰胺酶（EC 3.5.1.11）（先前用马来酸酐修饰）与丙烯酰胺经由交联剂进行共聚反应，获得了球形颗粒形式的酶制剂。与天然酶相比，固定化酰胺酶对加热更具抗性，对苄青霉素的亲和力较低，且受苯乙酸的抑制作用较小。其底物特异性和最适pH保持不变。
