頁籤選單縮合
題 名 | Production, Purification and Characterization of an Extracellular Catalase from Penicillium SP. TS-622=青黴菌TS-622菌株生產胞外雙氧水氧化酵素之純化及定性之研究 |
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作 者 | 林順富; 張鳴倫; | 書刊名 | 大同學報 |
卷 期 | 28 1998.11[民87.11] |
頁 次 | 頁359-366+477 |
分類號 | 368.87 |
關鍵詞 | 青黴菌TS-622菌株; 胞外雙氧水氧化酵素; |
語 文 | 英文(English) |
中文摘要 | 青黴菌TS-622菌株能在以麩皮固體培養基中生產胞外雙氧水氧化酵素。經一連續之色層管柱純化,酵素純度提高53倍。回收率有10。添加triton X-100可有效將酵素自麩皮固體培養基中萃取出,與不添加triton X-100相比,可提升酵素產量達100倍之多。純化酵素之分子量以分子篩管柱測定。分子量大約380,000。酵素最適反應pH及溫度為6至9之間及45℃。酵素在pH 4至11穩定,在50℃下維持60分仍具活性。酵素於407nm波長處有明顯吸收峰。酵素對雙氧水有極高之基質專一件,Km值為20.5 mM。NaN3、KCN及3-amino-1,2,4-trizo1e對酵素活性有抑制性。 |
英文摘要 | An extracellular catalase was purified from wheat bran culture of a soil-isolated Penicillium strain TS-622 by extracting the crude enzyme from mycelium and following successive chromatographies. The purity was enhanced by 53-fold with an overall yield of 10. The addition of Triton X-100 into the extraction buffer improved the extraction yield by 100 times. The molecular weight of this enzyme was 380,000 as determined by size exclusion chromatography and is composed of two hetero-subunits. The optimum pH was from 6 to 9 and optimum temperature was 45℃. The catalase was stable in the pH range of 4-11. It was stable up to 50℃ for lh at pH 6.6. The optical spectrum of the purified enzyme showed a soret band at 407 nm. Unlike catalase-peroxidase, this enzyme is highly specific toward hydrogen peroxide with a Km value of 20.5 mM. NaN,, K.CN and 3-amino-l,2,4- triazole effectively inhibit the catalytic function of the enzyme. |
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