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Sequence-based screening and characterization of cytosolic mandelate oxidase using oxygen as electron acceptor.
Liu, Shuang Ping; Liu, Rui Xia; Zhang, Liang; Shi, Gui Yang.
Afiliación
  • Liu SP; National Engineering Laboratory for Cereal Fermentation Technology, The Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, PR China.
  • Liu RX; National Engineering Laboratory for Cereal Fermentation Technology, The Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, PR China.
  • Zhang L; National Engineering Laboratory for Cereal Fermentation Technology, The Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, PR China.
  • Shi GY; National Engineering Laboratory for Cereal Fermentation Technology, The Key Laboratory of Industrial Biotechnology of Ministry of Education, Jiangnan University, Wuxi 214122, PR China. Electronic address: gyshi@jiangnan.edu.cn.
Enzyme Microb Technol ; 69: 24-30, 2015 Feb.
Article en En | MEDLINE | ID: mdl-25640721
Sequence-based screening was carried out to find a type of cytosolic mandelate oxidase that converted l-mandelate to phenylglyoxylate using oxygen as the final electron acceptor. The sequence features of the cytosolic mandelate oxidase were summarized, and were used in the screening process. Mandelate oxidases from Streptomyces coelicolor (HmoSC) and Amycolatopsis orientalis (HmoAO) were screened and then they were heterologously expressed and characterized. At pH 7.3 40 °C, the HmoAO showed kcat and Km values of 140 min(-1) and 10.2 mM, the HmoSC showed kcat and Km values of 105.1 min(-1) and 2.06 mM. The HmoSC was thermal stable and retained its 90% activity at 60 °C for up to 5 h, while HmoAO lost most of its activity at this temperature. The HmoSC could effectively catalyze the conversion of l-mandelate to phenylglyoxylate at higher temperature using oxygen as the final electron acceptor.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas de Alcohol / Ácidos Mandélicos Tipo de estudio: Diagnostic_studies / Screening_studies Idioma: En Revista: Enzyme Microb Technol Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Oxidorreductasas de Alcohol / Ácidos Mandélicos Tipo de estudio: Diagnostic_studies / Screening_studies Idioma: En Revista: Enzyme Microb Technol Año: 2015 Tipo del documento: Article Pais de publicación: Estados Unidos