| 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Flammeovirga sp. 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， MgSO4和β-Me对该酶有明显的促进作用，而CaCl2、MnCl2、ZnCl2、CoCl2、FeCl3、CuSO4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. |
| 关键词: 海洋生物学 Flammeovirga sp. 琼胶酶 分离纯化 酶学性质 |
| DOI：10.3969/J.ISSN.2095-4972.2016.01.014 |
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| 基金项目:海洋公益性行业科研专项经费资助项目(201105027) |
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| Purification and characterization of an agarase from Flammeovirga sp. SJP92 |
| HUANG Neng ping,RUAN Ling wei,SHI Hong |
| (Third Institute of Oceanography， SOA， Xiamen 361005， China) |
| Abstract: |
| 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 AgaB was about 70 kDa. The optimal pH and temperature for the best activity were 7-0 and 40℃， respectively. It showed the best stability under the optimal temperature. Furthermore， AgaB 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． |
| Key words: marine biology Flammeovirga sp. agarase purification enzymatic properties |
