从产L(+)-酒石酸的克雷伯氏菌中纯化和鉴定一种新型顺式环氧琥珀酸水解酶
Purification and characterization of a novel cis-epoxysuccinate hydrolase from Klebsiella sp. that produces L(+)-tartaric acid.
作者信息
Cheng Yongqing, Wang Li, Pan Haifeng, Bao Wenna, Sun Weirong, Xie Zhipeng, Zhang Jianguo, Zhao Yuhua
机构信息
College of Life Science, Institute of Biochemistry, Zhejiang University, Hangzhou, 310058, Zhejiang, People's Republic of China.
出版信息
Biotechnol Lett. 2014 Nov;36(11):2325-30. doi: 10.1007/s10529-014-1614-2. Epub 2014 Jul 22.
A strain of Klebsiella sp. BK-58 that produces cis-epoxysuccinate was screened and identified. This novel enzyme hydrolyzes cis-epoxysuccinate to L(+)-tartaric acid and was purified to homogeneity. Its molecular mass was 30.1 kDa determined by MALDI-TOF-MS analysis. It was stable up to 50 °C and from pH 5 to 11 with optima at 50 °C and pH 8.5. The enzyme was metal-independent and was strongly inhibited by 1 mM Cu(2+) and Ag(+), and 1 % (w/v) SDS. The K m , V max and turnover number (k cat ) values for cis-epoxysuccinate were 19.3, 2.24 mM min(-1) and 220 s(-1), respectively.
筛选并鉴定出一株产顺式环氧琥珀酸的克雷伯氏菌属菌株BK-58。这种新型酶将顺式环氧琥珀酸水解为L(+)-酒石酸，并纯化至同质。通过基质辅助激光解吸电离飞行时间质谱（MALDI-TOF-MS）分析测定其分子量为30.1 kDa。它在高达50°C且pH值为5至11的条件下稳定，最适温度为50°C，最适pH值为8.5。该酶不依赖金属，受到1 mM Cu(2+)、Ag(+)和1%（w/v）十二烷基硫酸钠（SDS）的强烈抑制。顺式环氧琥珀酸的米氏常数（K m）、最大反应速率（V max）和催化常数（k cat）值分别为19.3、2.24 mM min(-1)和220 s(-1)。
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