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海参体壁中α-1,4淀粉酶的分离纯化及性质
引用本文:张 杰,张永勤,罗彩华,刘征东,程袁芬,卢菲菲,张 童.海参体壁中α-1,4淀粉酶的分离纯化及性质[J].食品科学,2015,36(5):137-141.
作者姓名:张 杰  张永勤  罗彩华  刘征东  程袁芬  卢菲菲  张 童
作者单位:青岛科技大学化工学院,山东 青岛 266042
摘    要:通过采用匀浆、硫酸铵盐析、透析、DEAE-52阴离子交换层析、Sephacryl S-300凝胶层析等方法从海参体壁中分离纯化并得到了α-1,4淀粉酶。结果表明,该酶具有3条亚基链,分子质量约为420 k D;最适p H值为9.0,最适温度为80℃,90℃条件下保温30 min后仍有38%以上的相对酶活性,因此,该酶是一种具有较高热稳定性的碱性高温淀粉酶。K+、Fe3+和Mn2+对其有较强的抑制作用,Cu2+和Ca2+对其有较强的激活作用。

关 键 词:海参  自溶  淀粉酶  分离  纯化  热稳定性  

Purification and Characterization of α-1,4-Amylase in Body Wall of Sea Cucumber
ZHANG Jie,ZHANG Yongqin,LUO Caihua,LIU Zhengdong,CHENG Yuanfen,LU Feifei,ZHANG Tong.Purification and Characterization of α-1,4-Amylase in Body Wall of Sea Cucumber[J].Food Science,2015,36(5):137-141.
Authors:ZHANG Jie  ZHANG Yongqin  LUO Caihua  LIU Zhengdong  CHENG Yuanfen  LU Feifei  ZHANG Tong
Affiliation:College of Chemical Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
Abstract:α-1,4-Amylase was extracted and isolated from the body wall of sea cucumber by homogenization, salting out
with ammonium sulfate, dialysis, DEAE-52 anion exchange chromatography and Sephacryl S-300 gel chromatography
sequentially. The results showed that the purified enzyme had three subunit chains according to the SDS-PAGE, with
molecular weight of 420 kD; the optimum pH and temperature were 9.0 and 80 ℃; and the residual activity remained at least
38% after inactivation at 90 ℃ for 30 min. Therefore, this enzyme is a thermostable alkaline amylase. This amylase could be
strongly activated by K+, Fe3+ or Mn2+ and inhibited by Cu2+ or Ca2+.
Keywords:sea cucumber  autolysis  amylase  isolation  purification  thermostability  
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