壳聚糖固定L-天门冬酰胺酶的研究

Study on the Immobilization of L-Asparaginase on Chitosan

研究了以壳聚糖为载体，戊二醛为交联剂，固定化Ｌ－天门冬酰胺酶的最适条件，并对固定化天门冬酰胺酶的理化性质进行了初步探讨。分别从不同固定化程序、缓冲液及保护剂等方面进行了固定化天门冬酰胺酶的条件优化；固定化酶的活力回收可达２０％左右。固定化酶的最适范围变宽，由游离酶的最适ｐＨ＝４～６变为ｐＨ＝６～１０。连续使用６次后仍可基本维持固定化酶的活力。固定化酶对胃蛋白酶的水解性也较游离酶大大提高。

L-Asparaginase was immobilized on chitosan and crosslinked with glutaraldehyde. The optimum immobilization conditions and properties of immobilized enzyme were investigated. The activity recover of immobilized L-Asparaginase reached 20% or so when proper immobilization procedure, buffer solution and substrate were selected. The optimum pH range of immobilized enzyme was 6-10, which was much wider than that of soluble enzyme (4-6). The stability of immobilized enzyme in operation could be maintained fairly well after being repeatedly operated for six times. The resistance to pepsin hydrolysis was also improved greatly compared to that of soluble enzyme.