Purification and Some Properties of Glutaminase fromActinomucor taiwanensis,Starter of Sufu |
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Authors: | Jui-Mei Lu Roch-Chui Yu Cheng Chun Chou |
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Abstract: | Glutaminase of Actinomucor taiwanensis was purified approximately 96-fold with a yield of 18%, by sequential fractionation with ammonium sul-phate, anion exchange with DEAE-Sepharose CL-6B and gel filtration with Sephacryl S-200. The pH and temperature optima of purified glutaminase were 8·0 and 45°C, respectively. Glutaminase was stable at a temperature up to 35°C and at pH values of 6·0–8·0. The molecular weight was 80000 as determined from SDS-PAGE. The enzyme activity was markedly inhibited by HgCl2. In the presence of 100 g litre−1 NaCl, the enzyme activity was inhibited 50%. |
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Keywords: | glutaminase sufu Actinomucor taiwanensis |
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