Biochimie

Biochemical characterization and FAD-binding analysis of oleate hydratase from Macrococcus caseolyticus

YC Joo, KW Jeong, SJ Yeom, YS Kim, Y Kim, DK Oh

文献索引：Joo, Young-Chul; Jeong, Ki-Woong; Yeom, Soo-Jin; Kim, Yeong-Su; Kim, Yangmee; Oh, Deok-Kun Biochimie, 2012 , vol. 94, # 3 p. 907 - 915

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被引用次数: 30

摘要

A putative fatty acid hydratase gene from Macrococcus caseolyticus was cloned and expressed in Escherichia coli. The recombinant enzyme was a 68 kDa dimer with a molecular mass of 136 kDa. The enzymatic products formed from fatty acid substrates by the putative enzyme were isolated with high purity (> 99%) by solvent fractional crystallization at low temperature. After the identification by GC–MS, the purified hydroxy fatty acids were ...