Detection and partial characterization of γ-glutamyltranspeptidase from Cordyceps sinensis mycelia

China Biotechnology

2008, Vol. 28

Issue (10): 100-105 DOI:

Detection and partial characterization of γ-glutamyltranspeptidase from Cordyceps sinensis mycelia

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Abstract

γ-glutamyltranspeptidase was detected from the cultured mycelia of Cordyceps sinensis (CSGT). Km and Vmax of CSGT was 2.54×10-4 mol·L-1 and 0.1808 mol·L-1·min-1 respectively when L-Glutamic acid 5-(4-nitroanilide) (GpNA) and Glycyglycine was used as its substrate. CSGT was stable from pH 8.0 to 11.0 and at or below 20℃. It was optimally active at pH 9.0-10.0 and 30℃. A series of reducing reagents could activate CSGT, and metal cations such as Zn2+, Cu2+, Hg2+ , Mn2+ inhibited strongly activity of the enzyme, but K+, Ca2+, Mg2+ and Na+ at high concentrations had no effect on its activity, indicating that its active center could contain -SH.

Key words： γ-Glutamyltranspeptidase Cordyceps sinensis purification Characterization

Received: 09 May 2008 Published: 25 October 2008

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Cite this article:

. Detection and partial characterization of γ-glutamyltranspeptidase from Cordyceps sinensis mycelia. China Biotechnology, 2008, 28(10): 100-105.

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https://manu60.magtech.com.cn/biotech/ OR https://manu60.magtech.com.cn/biotech/Y2008/V28/I10/100

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