Production, purification and properties of γ-glutamyltranspeptidase from a newly isolated Bacillus subtilis NX-2 |
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Authors: | Qun Wu Hong Xu Lujia Zhang Jun Yao Pingkai Ouyang |
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Institution: | aCollege of Life Science and Pharmacy, Nanjing University of Technology, New Model Road No.5, Nanjing 210009, PR China |
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Abstract: | Production, purification and properties of γ-glutamyltranspeptidase from a newly isolated Bacillus subtilis NX-2 was investigated. At the optimum conditions for enzyme formation, a high level, 3.2 U/ml of γ-GTP was obtained. The extracellular γ-GTP from this strain was purified 111.15-fold to homogeneity from the culture supernatant by acetone precipitation, hydrophobic interaction chromatography and ion exchange chromatography. The purified enzyme was a heterodimer consisting of one large subunit (43 kDa) and one small subunit (32 kDa), and exhibited high activity at 40–60 °C, pH 8.0. It preferred basic amino acids as γ-glutamyl acceptor in transpeptidation, and the stereochemistry of the γ-glutamyl acceptor had no influence on the enzyme activity, which was different from other γ-GTPs reported. Furthermore, it was proved that γ-GTP of this strain could catalyze the transfer of l-glutamine to glycylglycine to synthesize Gln–Gly–Gly, which was promising for the synthesis of valuable γ-glutamyl peptides. |
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Keywords: | γ-Glutamyltranspeptidase B subtilis NX-2 Transpeptidation Purification Enzymatic characteristic |
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