蜡状芽孢杆菌ZJB-07112酰胺酶的分离纯化及其酶学性质

ZHANG Junwei; ZHENG Yuguo; SHEN Yinchu

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蜡状芽孢杆菌ZJB-07112酰胺酶的分离纯化及其酶学性质

更新时间：2025-12-10

- 蜡状芽孢杆菌ZJB-07112酰胺酶的分离纯化及其酶学性质
- CIESC Journal Issue 3, (2008)
- 作者机构：
  
  浙江工业大学生物工程研究所
- 作者简介：
- 基金信息：
- DOI：
  CLC：
- Online First：05 March 2008，
  
  Published：05 March 2008
- 稿件说明：
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ZHANG Junwei, ZHENG Yuguo, SHEN Yinchu. 蜡状芽孢杆菌ZJB-07112酰胺酶的分离纯化及其酶学性质[J]. CIESC Journal, 2008, (3).
DOI：

ZHANG Junwei, ZHENG Yuguo, SHEN Yinchu. 蜡状芽孢杆菌ZJB-07112酰胺酶的分离纯化及其酶学性质[J]. CIESC Journal, 2008, (3). DOI：

摘要

用一株蜡状芽孢杆菌新菌株ZJB-07112 (Bacillus cereus ZJB-07112)发酵生产酰胺酶，经超声波细胞破碎、High Q阴离子色谱、Phenyl-Sepharose疏水色谱等步骤获得了凝胶电泳均一的酰胺酶。用12.5% SDS-PAGE测得该酶的分子量约为60.6 kD。其N端氨基酸序列为ATIRPDDKAI。该酶水解反应的最适pH和最适温度分别为7.5和35 ℃。在pH 7.5条件下，该酶在50 ℃以上容易失活，60 ℃保温30 min后，仅保留10.8%的酶活。除了Hg+ 、Ag+等重金属离子和尿素外，其他金属离子和EDTA对该酶的活性影响不大。以丙烯酰胺为底物时，该酶的Km和Vmax值分别为2.64 mmol·L-1和0.6 μmol·min-1·ml-1。

Abstract

An amidase from a strain Bacillus cereus ZJB-07112 was purified to homogeneity by using sonication

anion-exchange chromatography

phenyl-sepharose chromatography.The molecular weight of amidase was estimated to be 60.6×103 by 12.5% SDS-PAGE. Its N-terminal sequence was ATIRPDDKAI. The optimum pH and temperature of the amidase for acrylamide were pH 7.5 and 35℃

respectively. The enzyme was unstable at a temperature over 50℃ and only 10.8% activity was retained after exposure to 60℃ for 30 min. Most of metal ions and EDTA had no significant effect on the enzyme activity

whereas Hg+，Ag+ and urea caused obvious inhibition.The K m and V max values of the amidase for acrylamide were 2.64 mmol·L-1 and 0.6 μmol·min-1·ml-1

respectively.

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