purification and properties of s-hydroxymethylglutathione dehydrogenase of paecilomyces variotii no. 5, a formaldehyde-degrading fungus拟青霉属s-hydroxymethylglutathione脱氢酶的纯化和属性variotii没有。.pdfVIP

下载本文档

3
0
约4.36万字
约 7页
2017-09-11 发布于上海
举报
版权申诉

purification and properties of s-hydroxymethylglutathione dehydrogenase of paecilomyces variotii no. 5, a formaldehyde-degrading fungus拟青霉属s-hydroxymethylglutathione脱氢酶的纯化和属性variotii没有。.pdf

1、本文档共7页，可阅读全部内容。
2、原创力文档（book118）网站文档一经付费（服务费），不意味着购买了该文档的版权，仅供个人/单位学习、研究之用，不得用于商业用途，未经授权，严禁复制、发行、汇编、翻译或者网络传播等，侵权必究。
3、本站所有内容均由合作方或网友上传，本站不对文档的完整性、权威性及其观点立场正确性做任何保证或承诺！文档内容仅供研究参考，付费前请自行鉴别。如您付费，意味着您自己接受本站规则且自行承担风险，本站不退款、不进行额外附加服务；查看《如何避免下载的几个坑》。如果您已付费下载过本站文档，您可以点击这里二次下载。
4、如文档侵犯商业秘密、侵犯著作权、侵犯人身权等，请点击“版权申诉”（推荐），也可以打举报电话：400-050-0827(电话支持时间：9:00-18:30)。
5、该文档为VIP文档，如果想要下载，成为VIP会员后，下载免费。
6、成为VIP后，下载本文档将扣除1次下载权益。下载后，不支持退款、换文档。如有疑问请联系我们。
7、成为VIP后，您将拥有八大权益，权益包括：VIP文档下载权益、阅读免打扰、文档格式转换、高级专利检索、专属身份标志、高级客服、多端互通、版权登记。
8、VIP文档为合作方或网友上传，每下载1次，网站将根据用户上传文档的质量评分、类型等，对文档贡献者给予高额补贴、流量扶持。如果你也想贡献VIP文档。上传文档

purification and properties of s-hydroxymethylglutathione dehydrogenase of paecilomyces variotii no. 5, a formaldehyde-degrading fungus拟青霉属s-hydroxymethylglutathione脱氢酶的纯化和属性variotii没有。

Fukuda et al. AMB Express 2012, 2:32 /content/2/1/32 ORIGINAL ARTICLE Open Access Purification and properties of S-hydroxymethylglutathione dehydrogenase of Paecilomyces variotii no. 5, a formaldehyde-degrading fungus * Ryohei Fukuda, Kazuhiro Nagahama, Kohsai Fukuda, Keisuke Ekino, Takuji Oka and Yoshiyuki Nomura Abstract S-hydroxymethylglutathione dehydrogenase from Paecilomyces variotii No. 5 strain (NBRC 109023), isolated as a formaldehyde-degrading fungus, was purified by a procedure that included ammonium sulfate precipitation, DEAE- Sepharose and hydroxyapatite chromatography and isoelectrofocusing. Approximately 122-fold purification was achieved with a yield of 10.5%. The enzyme preparation was homogeneous as judged by sodium dodecyl polyacrylamide gel electrophoresis (SDS). The molecular mass of the purified enzyme was estimated to be 49 kDa by SDSand gel filtration, suggesting that it is a monomer. Enzyme activity was optimal at pH 8.0 and was stable in the range of pH 7.0– 10. The optimum temperature for activity was 40°C and the enzyme was stable up to 40°C. The isoelectric point was pH 5.8. Substrate specificity was very high for formaldehyde. Besides formaldehyde, the only aldehyde or alcohol tested that served as a substrate was pyruvaldehyde. Enzyme activity was enhanced by several divalent cations such as Mn2+ (179%), Ba2+ (132%), and Ca2+ (112%) but was completely inhibited by Ni2+, Fe3+, Hg2+, p-chloromercuribenzoate (PCMB) and cuprizone. Inactivation of the enzyme by sulfhydryl reagents (Hg2+ and PCMB) indicated that the sulfhydryl group of the enzyme is essential for catalytic activity. Keywords: S-hydroxymethylglutathione dehydrogenase, Enzyme purification, Formaldehy