Flammeovirga sp.SJP92琼脂酶的分离纯化及其酶学性质  

Purification and characterization of an agarase from Flammeovirga sp. SJP92

作　　者：黄能平 阮灵伟[1] 施泓[1] 

机构地区：[1]国家海洋局第三海洋研究所,福建厦门361005

出　　处：《应用海洋学学报》2016年第1期116-121,共6页Journal of Applied Oceanography

基　　金：海洋公益性行业科研专项经费资助项目(201105027)

摘　　要：琼胶酶是一类能够降解琼脂糖生成琼胶寡糖的酶类,具有广泛的应用范围.从海洋性高产琼胶酶菌株Flammeovirgasp.SJP92的发酵液经硫酸铵沉淀,DEAE-琼脂糖离子层析,分离纯化获得了一个分子量约为70KDa的琼胶酶AgaB.经过酶学性质分析,它的最适pH值为7.0,最适温度为40℃,在最适温度下能够保持较好的稳定性.进一步的分析表明,MgSO_4和β-Me对该酶有明显的促进作用,而CaCl_2、MnCl_2、ZnCl_2、CoCl_2、FeCl_3、CuSO_4等则会强烈抑制它的活性.此外,通过产物分析表明,该酶能够通过内切作用将琼脂糖最终降解成6糖和4糖.AgaB的分离纯化及其酶学性质分析为其工业应用奠定了基础.Agarases are the enzymes that can catalyze the hydrolysis of agar,and are widely used in some fields. In the present study,an agarase was purified from a high agarase production marine bacterium,Flammeovirga sp.SJP92 by ammonium sulfate precipitation and DEAE-Sepharose Fast Flow. The molecular mass of the agarase Aga B was about 70 k Da. The optimal p H and temperature for the best activity were 7. 0 and 40℃,respectively. It showed the best stability under the optimal temperature. Furthermore,Aga B was obviously activated by MgSO4 and β-Me,while strongly inhibited by CaCl2,MnCl2,ZnCl2,CoCl2,FeCl3 and CuSO4. Besides,it degraded agarose by endo-type hydrolysis with end products of neoagarotetraose and neoagarohexaose. Our study lays a better foundation for its industry application.

关 键 词：海洋生物学 Flammeovirga sp. 琼胶酶 分离纯化 酶学性质 

分 类 号：P735[天文地球—海洋生物学]