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枯草杆菌AS1.398中性蛋白酶在蟹壳几丁质上的固定化作用

IMMOBILIZATION OF BACILLUS SUBSTILIS AS 1.398 NEUTRAL PROTEASE ON CRAB CHITIN

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【作者】 申炳华; 冯涛; 刘鸿铭;

【Author】 Shen Binghua,Feng Tao and Liu Hongming

【机构】 北京师范大学生物系; 北京师范大学生物系;

【摘要】 1.蟹壳通过酸碱处理后,可制得白色的比较纯净的几丁质。2.用戊二醛把枯草杆菌AS1.398中性蛋白酶共价结合到几丁质上,并探索了固定化条件。3.固定化的枯草杆菌AS1.398中性蛋白酶和天然酶比较,最适温度向高温方向移动约3℃。最适pH基本上没有变化。底物为酪蛋白时的K_m值略变小。热稳定性和贮存稳定性明显增加,尤其在底物和Ca~存在条件下,这种稳定性更为加强。

【Abstract】 White and purer chitin was prepared by treatment of crab shell with acid and alkali. Bacillus subtilis AS1.398 neutral protease was covalently bound on chitin by using glutaraldehyde as a cross-linking ageat and the conditions of immobilization were investigated. Some properties of the immobilized and native enzyme were compared. It was found that the optimum temperature of impsobilized enzyme was 3℃ higher than that of native one but their optimum pH were almost the same. K_m value of immobilized earyme was smaller when casein used as a substrate. After immobilization the stability of the enzyme against heat or in process of preservation increased distinctly, especially in the presence of its substrate and Ca~.

  • 【文献出处】 北京师范大学学报(自然科学版) ,Journal of Beijing Normal University(Natural Science) , 编辑部邮箱 ,1986年01期
  • 【被引频次】14
  • 【下载频次】76
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