|本期目录/Table of Contents|

[1]孙倩倩,潘瑶,姚忠,等.嗜热菌Bacillus fordii 3-2海因酶的纯化及性质[J].生物加工过程,2007,5(04):32-36.[doi:10.3969/j.issn.1672-3678.2007.04.007]
 SUN Qian-qian,PAN Yao,YAO Zhong,et al.Purification and characterization of hydantoinase from thermophilus Bacillus fordii 3-2[J].Chinese Journal of Bioprocess Engineering,2007,5(04):32-36.[doi:10.3969/j.issn.1672-3678.2007.04.007]
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嗜热菌Bacillus fordii 3-2海因酶的纯化及性质()
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《生物加工过程》[ISSN:1672-3678/CN:32-1706/Q]

卷:
5
期数:
2007年04期
页码:
32-36
栏目:
出版日期:
2007-11-30

文章信息/Info

Title:
Purification and characterization of hydantoinase from thermophilus Bacillus fordii 3-2
作者:
孙倩倩潘瑶姚忠何冰芳
南京工业大学, 制药与生命科学学院, 南京, 210009
Author(s):
SUN Qian-qian PAN Yao YAO Zhong HE Bing-fang
关键词:
海因酶Bacillus fordii 3-2纯化酶学性质
分类号:
Q55
DOI:
10.3969/j.issn.1672-3678.2007.04.007
摘要:
对自行筛选的海因酶法L-苯丙氨酸生产菌株Bacillus fordii 3-2中的海因酶进行了分离纯化及相关性质研究.该海因酶协同L-氨甲酰水解酶是海因酶法生产L-氨基酸的关键酶.B.fordii 3-2菌悬液经压力破碎离心后取上清液为粗酶液,粗酶液通过硫酸铵分级沉淀、Phenyl FF(high sub) 疏水层析以及Source 15Q离子交换层析,经SDS-PAGE分析达到电泳纯,亚基相对分子质量为55×103,海因酶的纯化回收率为20.5%,纯化倍数为149.23.该海因酶在pH 8.0~10.0的范围内具有较高的活性,在45~70℃具有很高的酶活力, 最适反应pH和温度分别为10.0 ℃和65 ℃.纯酶易氧化失活,DTT对该酶有一定的保护作用.二价金属离子,Mn2+、Co2+ 及Fe2+对酶活性有显著的促进作用,而Ca2+、Cu2+等对酶活性有抑制作用.相关研究可为该菌株及海因酶的进一步开发与应用提供理论指导.

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相似文献/References:

[1]梅艳珍,何冰芳,欧阳平凯.海因酶热稳定性及底物特异性研究进展[J].生物加工过程,2005,3(03):24.[doi:10.3969/j.issn.1672-3678.2005.03.005]
 MEI Yan-zhen,HE Bing-fang,OUYANG Ping-kai.Progress in study on thermostability and substrate specificity of hydantoinase[J].Chinese Journal of Bioprocess Engineering,2005,3(04):24.[doi:10.3969/j.issn.1672-3678.2005.03.005]
[2]丁成勇,徐晓滢,马喆,等.Eupergit C250L固定化D-海因酶及其催化性质[J].生物加工过程,2006,4(04):41.[doi:10.3969/j.issn.1672-3678.2006.04.009]
 DING Cheng-yong,XU Xiao-ying,MA Zhe,et al.Immobilization of D-hydantoinase on Eupergit C250L and properties of the immobilized biocatalyst[J].Chinese Journal of Bioprocess Engineering,2006,4(04):41.[doi:10.3969/j.issn.1672-3678.2006.04.009]

备注/Memo

备注/Memo:
基金项目:国家重点基础研究发展计划(973计划),国家自然科学基金
更新日期/Last Update: 1900-01-01