Characterization of two glycoside hydrolase family 36 伪-galactosidases: Novel transglycosylation activity, lead-zinc tolerance, alkaline and multiple pH optima, and low-temperature activity
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- 作者：Junpei Zhoua ; b ; c ; d ; 1 ; Qian Lub ; 1 ; Rui Zhanga ; b ; c ; d ; Yiyan Wangb ; Qian Wua ; b ; c ; d ; Junjun Lia ; b ; c ; d ; Xianghua Tanga ; b ; c ; d ; Bo Xua ; b ; c ; d ; Junmei Dinga ; b ; c ; d ; Zunxi Huanga ; b ; c ; d ; huangzunxi@163.com" class="auth_mail" title="E-mail the corresponding author
- 关键词：Transglycosylation ; 伪-Galactosidase ; Lead&ndash ; zinc tolerance ; pH optimum ; Low-temperature activity
- 刊名：Food Chemistry
- 出版年：2016
- 出版时间：1 March 2016
- 年：2016
- 卷：194
- 期：Complete
- 页码：156-166
- 全文大小：2334 K
文摘
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A GH 36 伪-galactosidase from Streptomyces sp. HJG4 showed low-temperature activity.
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The Streptomyces 伪-galactosidase (AgaAHJG4) showed alkaline and multiple pH optima.
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A GH 36 伪-galactosidase from Mesorhizobium sp. JB07 was lead–zinc tolerant.
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The two enzymes showed transglycosylation activity but required different acceptors.
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Potential sequence– and structure–function relationships of AgaAHJG4 were presumed.