Zn^(2+)对棉铃虫N-乙酰-β-D-氨基葡萄糖苷酶活力与性质的影响  

EFFECT OF Zn 2+ ON ACTIVITY AND PROPERTIES OF β-N-ACETYL-D-GLUCOSAMINIDASE FROM HELICOVERPA ARMIGERA PUPAE *

作　　者：黄小红[1] 陈清西[2] 王君[2] 谢雪清[1] 关雄[1] 

机构地区：[1]福建农林大学生物农药与化学生物学教育部重点实验室 [2]厦门大学生命科学学院教育部细胞生物学与肿瘤细胞工程重点实验室,福建厦门361005

出　　处：《应用与环境生物学报》2005年第6期711-713,共3页Chinese Journal of Applied and Environmental Biology

基　　金：国家高技术研究发展计划项目(2002AA245011);福建省自然科学基金(Z0516010)~~

摘　　要：以棉铃虫蛹为材料,经分离纯化获得棉铃虫N乙酰βD氨基葡萄糖苷酶制剂;研究了Zn2+对棉铃虫N乙酰βD氨基葡萄糖苷酶(EC3.2.1.14)活力与性质的影响.结果表明,Zn2+对酶活力有抑制作用,酶活力丧失一半的Zn2+浓度(IC50)为1.3mmol/L.进一步研究Zn2+的抑制作用动力学,发现Zn2+对该酶的抑制作用是一种可逆过程,抑制机理表现为竞争型,抑制常数KI为1.158mmol/L.Zn2+不会影响酶的酸碱稳定性,但有Zn2+存在时,在30～40范围内,酶是稳定的,温度高于50℃后,随着Zn2+浓度的增加,酶的温度稳定性也相对增加.A β-N-Acetyl-D-glucosaminidase （EC3.2.1.52） was purified from the pupae of Helieoverpa armigera . The effect of Zn^2＋ on β-N-acetyl-D-glucosaminidase （ NAGase, EC3.2.1.52 ） from H. armigera was studied. The result showed that Zn^2＋ inhibited the enzyme. The inhibitory kinetics of Zn^2＋ on the enzyme showed that Znz^2＋ was a reversible competitive inhibitor of the enzyme, and the inhibition constant （K1） was determined to be 1. 158 mmol/L. Zn^2＋ couldnt affect pH stability of the enzyme. However, in the presence of Zn^2＋ , the enzyme was stable between 30 and 40℃, and when the temperature was above 50℃, the thermostahility of enzyme increased with the increasing of the concentration of Zn^2＋. Fig 5, Ref 10

关 键 词：棉铃虫 N-乙酰-Β-D-氨基葡萄糖苷酶 ZN^2+ 活力 性质 

分 类 号：S482.91[农业科学—农药学]