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Abstract
A depolymerase capable of decomposing γ-polyglutamic acid was formed when Bacillus natto was infected with bacteriophage. By disrupting prematurely the infected bacteria, it was shown that the enzyme was induced at about 7 min after phage infection and reached to a maximum level on lysis of the infected bacteria. The enzyme activity was not detected in the uninfected bacteria. The phage particles had no enzyme activity. Preliminary studies on the enzymatic hydrolyzates by paper chromatography revealed that this enzyme cleaved γ-polyglutamic acid to small peptides by the endopeptidase action.
Abstract
Phage-induced γ-polyglutamic acid depolymerase was purified about 1000 fold by Sephadex G-75 and DEAE-cellulose column chromatographies and Sephadex G-200 gel filtration. Using dl-γ-polyglutamic acid (PGA) produced by the host bacterium as a substrate, the enzymatic hydrolysis was studied. The enzyme decomposed rapidly PGA to small peptides with the endopeptidase action, but to glutamic acid with difficulty. Main two products were identified through their DNP-derivatives and proved to be dl-di- and tri-γ-glutamyl peptides. The enzyme could not completely cleave the PGA chain and about 40% of PGA remained without hydrolysis.