南美白对虾体壁几丁质酶的理化特性研究  

Studies on the Properties of Chitinase from the Integument of the Prawn(Penaeus vannamei)

作　　者：林建城[1] 林俊兵[1] 陈郁花[1] 林秀春[1] 

机构地区：[1]莆田学院环境与生命科学系,莆田351100

出　　处：《生物技术通报》2007年第4期169-172,共4页Biotechnology Bulletin

基　　金：福建省教育厅科技项目(JB04175);莆田学院科研基金资助项目(No.2004031)

摘　　要：报道南美白对虾体壁几丁质酶(EC3.2.1.14)的理化性质。结果表明,酶的最适pH值为5.6,最适温度为55℃。该酶在pH5.0～6.2区域较稳定,而在pH>7和pH<4.6下失活加快;在50℃以下处理1h,酶活力保持稳定,高于55℃,酶稳定性较差,很快失活。研究金属离子对酶活力影响,结果表明:Li+、Na+、K+、Mg2+和Fe2+等对该酶活力没有任何效应;Ca2+、Ba2+对酶有激活作用,Cu2+、Co2+对酶的效应先表现为激活后转为抑制作用;Ni2+、Zn2+、Mn2+、Al3+、Fe3+、Hg2+、Pb2+和Cd2+对该酶活力均具有不同程度的抑制作用,以Hg2+的抑制作用最显著,10mmol/L的Hg2+可抑制酶活力95.6%。A study on the properties of chitinase （EC3.2.1.14）ffom the integument of the Prawn（Penaeus vannamei）was surveyed.The optimum pH and optimum temperature of the enzyme for the hydrolysis of colloidal chitin （enzyme substrate）were determined to be pHS.6 and 55℃,respectively.The stability of the enzyme was investigated,and the results showed that the enzyme was stable in a pH range from 5.0 to 6.2 and at temperatures 〈50℃.The effects of metal ions on the enzyme were also studied.Li^＋,Na^＋,K^＋,Mg^2＋ and Fe^2＋ had no any effect on the enzyme activity while Ca^2＋ and Ba^2＋ activated the enzyme,The results indicated that Cu^2＋,Co^2＋ activated the enzyme at low concentration,but they inactivated it at high concentrations.Ba^2＋,Al^3＋,Fe^3＋,Zn^2＋,Co^2＋,Cd^2＋,Hg^2＋,Pb^2＋ and Cu^2＋ inhibited the enzyme.The inhibitory effect of Hg^2＋ was the most potent, 10 mmol/L Hg^2＋ led to the enzyme activity to lose by 95.6%.

关 键 词：海洋生物 几丁质酶 南美白对虾 理化性质 金属离子 

分 类 号：Q55[生物学—生物化学]