Abstract
γ-Glutamyltranspeptidase (GGT) was purified from a solid culture of Penicillium roqueforti IFO 4622 to electrophoretic homogeneity. It has a molecular weight of 120,000 and consists of two different subunits with molecular weights of 55,000 and 66,000. The GGT showed eleven times higher transpeptidation activity than the hydrolytic activity. The optimum pH region was 8.0 to 9.0 for both transpeptidation and hydrolysis reactions. In the transpeptidation reaction, various amino compounds were found to act as γ-glutamyl acceptors when l-γ-glutamyl-ρ-nitroanilide was used as the γ-glutamyl donor. The enzyme was less heat stable but much more tolerant to the inhibition by NaCl than Aspergillus oryzae GGT.
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