Identification and characterization of an acetyl esterase from Paenibacillus sp. XW-6-66 and its novel function in 7-aminocephalosporanic acid deacetylation
Identification and characterization of an acetyl esterase from Paenibacillus sp. XW-6-66 and its novel function in 7-aminocephalosporanic acid deacetylation
复制标题
类芽孢杆菌乙酰酯酶的鉴定和表征。
DOI：
10.1007/s10529-019-02709-y
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发表时间：
2019-07
期刊：
影响因子：
--
通讯作者：
Zuni Huang
中科院分区：
文献类型：
--
作者：
Junmei Ding;Yang Zhou;Hujie Zhu;Ming Deng;Liangchuan Long;Yunjuan Yang;Qian Wu;Zuni Huang
目的：从类芽孢杆菌（Paenibacillus sp.）XW-6 - 66中获得一种新的乙酰酯酶，并将其应用于7-氨基头孢烷酸（7-ACA）的脱乙酰化反应。AesZY属于α/β水解酶超家族中的乙酰酯酶（Aes）家族，其催化三联体为Ser 114-Asp 203-His 235，含有Gly-X-Ser-X-Gly基序。在pH8.0和40 °C下检测到AesZY的最大活性。AesZY在5.0 ~ 12.0的不同pH值范围内稳定，并对几种金属离子具有耐受性。AesZY对7-ACA的脱乙酰活性约为7.5U/mg，Kcat/Km值为2.04 s-1 mM-1。结论：Aes家族的新乙酰酯酶具有潜在的生物工程应用价值。
Objectives:To obtain a new acetyl esterase from Paenibacillus sp. XW-6-66 and apply the enzyme to 7-aminocephalosporanic acid (7-ACA) deacetylation.Results:The acetyl esterase AesZY was identified from Paenibacillus sp. XW-6-66, and its enzymatic properties were investigated. With the putative catalytic triad Ser114-Asp203-His235, AesZY belongs to the Acetyl esterase (Aes) family which is included in the α/β hydrolase superfamily and contains the consensus Gly-X-Ser-X-Gly motif. The maximum activity of AesZY was detected at pH 8.0 and 40 °C. AesZY was stable at different pH values ranging from 5.0 to 12.0, and was tolerant to several metal ions. Furthermore, the deacetylation activity of AesZY toward 7-ACA was approximately 7.5 U/mg, and the Kcat/Kmvalue was 2.04 s-1mM-1.Conclusions:Our results demonstrate the characterization of a new acetyl esterase belonging to the Aes family with potential biotechnological applications.
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影响因子：
2.9
作者：
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通讯作者：
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DOI：
10.1016/j.ijbiomac.2016.12.061
发表时间：
2017-03
影响因子：
8.2
作者：
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