Structure of the Hydrolyzed Product (F-2) Released from γ-Polyglutamic Acid by γ-Glutamyl Hydrolase YwtD ofBacillus subtilis

Phylogeny of γ-polyglutamic acid-producing Bacillus strains isolated from fermented soybean foods manufactured in Asian countries

“…The ratios of D-glutamic acid to L-glutamic acid in PGA were different in B. subtilis and B. amyloliquefaciens ( Table 2), indicating that the ratio of Dglutamic acid to L-glutamic acid in PGA of the latter is higher than that of the former. We previously proposed the PGA structure of B. subtilis NBRC 16449, a nattoproducing strain (Chunhachart et al, 2006a;Suzuki and Tahara, 2003). The PGA is composed of a highmolecular-mass region (F-1) with only L-glutamic acid and a 2.0-kDa low-molecular-mass region (F-2) with Dand L-glutamic acids in an 80 : 20 ratio, and F-2 consists of a D-glutamic acid cluster in the N-terminus and two or three consecutive L-glutamic acids near the Cterminus.…”

Phylogeny of γ-polyglutamic acid-producing Bacillus strains isolated from a fermented locust bean product manufactured in West Africa

“…3). Strains B. amyloliquefaciens NBRC 15535 T , B. subtilis NBRC 16449, B. licheniformis NBRC 12107, B. pumilus NBRC 12094 and L. sphaericus NBRC 3525 produced high-molecular-mass PGA, among which the structure of PGA produced by B. subtilis NBRC 16449 was proposed (Chunhachart et al, 2006a;Suzuki and Tahara, 2003), but B. atrophaeus NBRC 15539 T and B. mojavensis NBRC 15718 T produced low-molecular-mass PGA, the structure of which is now under investigation.…”

Characterization of γ-Glutamyl Hydrolase Produced byBacillussp. Isolated from Thai Thua-nao

“…MO) 13,14) hydrolyzed the product, and carboxypeptidase G (-L-glutamyl hydrolase, Sigma) 15) also degraded it, indicating that it contains L-glutamic acid in both the N-and C-termini. Furthermore, the 20-kDa product was hydrolyzed by YwtD, 13) a -glutamyl hydrolase that cleaves the -glutamyl linkage between D-and Dglutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region of PGA, into two products of about 20 kDa and about 2 kDa in molecular mass.…”

“…Furthermore, the 20-kDa product was hydrolyzed by YwtD, 13) a -glutamyl hydrolase that cleaves the -glutamyl linkage between D-and Dglutamic acid recognizing adjacent L-glutamic acid toward the N-terminal region of PGA, into two products of about 20 kDa and about 2 kDa in molecular mass. This suggests that the 20-kDa PGA produced byglutamyl hydrolase of Bacillus sp.…”

“…CMU29. 13) On the other hand, the Myrothecium enzyme purified from the culture broth has been proposed as a -L-glutamyl hydrolase because this enzyme degraded the Bacillus PGA into two hydrolyzed products, a highmolecular-mass product (20-40 kDa with D-and Lglutamic acids in ratio of 76:24) and a 0.5-kDa product with only L-glutamic acid. -Glutamyl hydrolase, described here, hydrolyzed chemically synthesized oligo--L-PGAs but did not completely cleave theglutamyl linkage between the L-and L-glutamic acids of the Bacillus PGA, which is similar to that of the Myrothecium enzyme, suggesting that the enzyme acts differently on chemically synthesized oligo PGAs and Bacillus PGA.…”