2006 Volume 70 Issue 11 Pages 2779-2782
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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