Abstract
γ-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.
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Chunhachart, O., Itoh, T., Sukchotiratana, M., Tanimoto, H., & Tahara, Y. (2006). Characterization of γ-glutamyl hydrolase produced by Bacillus sp. isolated from Thai Thua-nao. Bioscience, Biotechnology and Biochemistry, 70(11), 2779–2782. https://doi.org/10.1271/bbb.60280
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