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商品果胶酶(Aspergillus niger)的催化动力学研究
引用本文:林建城,杨文杰,朱丽华,王志鹏,陈国强.商品果胶酶(Aspergillus niger)的催化动力学研究[J].甘肃农业大学学报,2006,41(4):81-85.
作者姓名:林建城  杨文杰  朱丽华  王志鹏  陈国强
作者单位:莆田学院环境与生命科学系,福建,莆田,351100
基金项目:莆田市科技计划项目(2005N12)资助,福建省教育厅科技项目(JA05320)资助.
摘    要:研究了商品果胶酶的催化动力学特性.结果表明:果胶酶的最适pH为3.8,最适温度为50℃,酶在pH 3.4~4.2区域较稳定,在pH>4.5与pH<3.0下很快失活;酶在50℃以内具有较好的热稳定性,温度升高,酶的热稳定性下降,65℃下热变性2 h,酶活力降低80%.酶促反应动力学符合米氏双曲线方程,测得果胶酶水解果胶的米氏常数Km=(5.16±0.13)mg/mL,最大反应速度Vmax=(2.73±0.02)μg/(mL.min).Na+和K+对酶活力没有任何效应,0.1mmol/L Ca2+可使酶活力提高22.8%,5.0 mmol/L Zn2+对果胶酶活力的抑制达到17.4%,Mg2+、Mn2、Co2+、Hg2+和Ag+对果胶酶活力影响不大,Cu2+和Fe3+对果胶酶活力影响较大,浓度为5.0 mmol/L时,对果胶酶的抑制可分别达到88.9%和100%.

关 键 词:果胶酶  催化动力学  酶活力  稳定性  金属离子
文章编号:1003-4315(2006)04-0081-05
收稿时间:2006-03-03
修稿时间:2006-03-03

Study on catalytic kinetics of commercial pectinase from Aspergillus niger
LIN Jian-cheng,YANG Wen-jie,ZHU Li-hua,WAN Zhi-peng,CHEN Guo-qiang.Study on catalytic kinetics of commercial pectinase from Aspergillus niger[J].Journal of Gansu Agricultural University,2006,41(4):81-85.
Authors:LIN Jian-cheng  YANG Wen-jie  ZHU Li-hua  WAN Zhi-peng  CHEN Guo-qiang
Abstract:The characteristics in catalytic kinetics of commercial pectinase from Aspergillus niger were determineded.The results showed that the optimum pH and optimum temperature of the enzyme for the hydrolysis of pectin(enzyme substrate)were pH 3.8 and 50 ℃,respectively.The behavior of the enzyme during hydrolysis of pectin followed Michaelis-Menten kinetics,with K_(m)=5.16±0.13 mg·mL~(-1)and V_(max)=2.73±0.02 μg·mL~(-1)·min~(-1),at pH 3.8 and 50 ℃.The stability of the enzyme was investigated,and the results showed that the enzyme was stable in a pH range from 3.4 to 4.2 and at temperatures<50 ℃.The effects of metal ions on the enzyme were also studied.Na~(+) and K~(+)had no influence on enzyme activity.Ca~(2+) in the concentration of 0.1 mmol/L increase activity of the enzyme,while Mg~(2+),Mn~(2+),Co~(2+),Ni~(2+),Hg~(2+),Ag~(+),Zn~(2+),Cu~(2+) and Fe~(3+) showed various degrees of inhibitory effects on the enzyme in the concentration of 5.0 mmol/L,among which Zn~(2+) in the concentration of 5.0 mmol/L inhibited activity of the enzyme by 17.4 %,and Cu~(2+) by 88.9 %,Fe~(3+) by 100 %.
Keywords:pectinase  catalytic kinetics  enzyme activities  stability  metal ions
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