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紫色红曲霉中新型酯酶ESM1的纯化及其酶学特性研究
引用本文:张玉,周冉冉,李可心,黄宇,陈茂彬. 紫色红曲霉中新型酯酶ESM1的纯化及其酶学特性研究[J]. 中国酿造, 2018, 37(12): 137. DOI: 10.11882/j.issn.0254-5071.2018.12.027
作者姓名:张玉  周冉冉  李可心  黄宇  陈茂彬
作者单位:(1.湖北工业大学 生物工程与食品学院 发酵工程教育部重点实验室,湖北 武汉 430068;2.工业发酵湖北省协同创新中心,湖北 武汉 430068;3.工业微生物湖北省重点实验室,湖北 武汉 430068)
基金项目:湖北省科技支撑计划项目(2015BAA154);“十三五”国家重点研发计划项目(2016YFD040050)
摘    要:
该研究以白酒大曲中筛选出的一株高产酯酶菌株HQ为研究对象,采用分子生物学对其进行菌种鉴定。通过硫酸铵二级沉淀、丁基琼脂糖凝胶柱和Superdex G-200柱对其所产的酯酶进行纯化,并进行N-端序列、质谱和酶学性质分析。结果表明,菌株HQ被鉴定为紫红曲霉(Monascus purpureus),经纯化获得一个分子质量为60 kDa的酯酶,命名为ESM1。酯酶ESM1具有一段酸性蛋白酶的肽段序列,最适温度为60 ℃、最适pH值为7.0,在温度为50 ℃的环境和中性环境中表现出良好的稳定性。Zn2+、Ca2+和Na+对ESM1有促进作用,其中Zn2+促进作用最高,Cu2+、Mg2+、Fe2+和Mn2+有抑制作用,其中Cu2+的抑制作用最强。

关 键 词:紫色红曲霉  酯酶  纯化  酶学性质  

Purification and characterization of a new esterase ESM1 from Monascus purpureus
ZHANG Yu,ZHOU Ranran,LI Kexin,HUANG Yu,CHEN Maobin. Purification and characterization of a new esterase ESM1 from Monascus purpureus[J]. China Brewing, 2018, 37(12): 137. DOI: 10.11882/j.issn.0254-5071.2018.12.027
Authors:ZHANG Yu  ZHOU Ranran  LI Kexin  HUANG Yu  CHEN Maobin
Affiliation:(1.Key Lab of Fermentation Engineering of Ministry of Education, College of Biological Engineering and Food, Hubei University of Technology, Wuhan 430068, China; 2.Hubei Collaborative Innovation Center for Industrial Fermentation, Wuhan 430068, China; 3.Hubei Key Lab of Industrial Microbiology, Wuhan 430068, China)
Abstract:
Using a strain HQ with high-yield esterase screened from Baijiu (Chinese liquor) Daqu as the research object, the strain was identified by molecular biology. The esterase produced by the strain HQ was purified by ammonium sulfate two-stage precipitation, butyl agarose gel column and Superdex G-200 column, and analyzed by N-terminal sequence, mass spectrometry and enzymatic properties. The results showed that the strain HQ was identified as Monascus purpureus, and the esterase with a molecular weight of 60 kDa was obtained by purification, named ESM1. The esterase ESM1 had a peptide sequence of an acid protease, and the optimum temperature and pH of the esterase ESM1 were 60 ℃, 7.0, respectively. The esterase ESM1 had good stability in the environments of 50 ℃ and neutral environments. The esterase ESM1 could be promoted by Zn2+, Ca2+ and Na+, among which the promoting effect of Zn2+ was the strongest, and be inhibited by Cu2+, Mg2+, Fe2+ and Mn2+, among which the inhibiting effect of Cu2+ was the strongest.
Keywords:Monascus purpureus  esterase  purification  enzymatic property  
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