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dc.contributor.authorOrawan Chunhacharten_US
dc.contributor.authorTakenori Itohen_US
dc.contributor.authorMorakot Sukchotiratanaen_US
dc.contributor.authorHiroyuki Tanimotoen_US
dc.contributor.authorYasutaka Taharaen_US
dc.description.abstractγ-Glutamyl hydrolase with a molecular mass of 28 kDa was purified from the culture broth of Bacillus sp. isolated from Thai Thua-nao, a natto-like fermented soybean food. The purified enzyme hydrolyzed chemically synthesized oligo-γ-L-glutamates but not oligo-γ-D-glutamates and degraded γ-polyglutamic acid to a hydrolyzed product of only about 20 kDa (with D- and L-glutamic acid in a ratio of 70:30), suggesting that the enzyme is a γ-glutamyl hydrolase that cleaves the γ-glutamyl linkage between L- and L-glutamic acid of γ-polyglutamic acid.en_US
dc.subjectAgricultural and Biological Sciencesen_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.subjectChemical Engineeringen_US
dc.subjectImmunology and Microbiologyen_US
dc.titleCharacterization of γ-glutamyl hydrolase produced by Bacillus sp. isolated from Thai Thua-naoen_US
article.title.sourcetitleBioscience, Biotechnology and Biochemistryen_US
article.volume70en_US University Corporation Shizuoka Universityen_US Mai Universityen_US Co Incen_US
Appears in Collections:CMUL: Journal Articles

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