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首页> 外文期刊>Journal of Microbiology, Biotechnology and Food Sciences >CHARACTERIZATION OF TYROSINASE ENZYME FROM NATIVE BACILLUS MEGATERIUM SP. STRAIN M36
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CHARACTERIZATION OF TYROSINASE ENZYME FROM NATIVE BACILLUS MEGATERIUM SP. STRAIN M36

机译：天然芽孢杆菌SP中酪氨酸酶的表征应变M36

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摘要

Tyrosinase is a type 3 copper-containing enzyme that catalyzes the conversion of l-tyrosine to L-DOPA and finally to melanin. In this study tyrosinase enzyme from native Bacillus megaterium sp. strain M36, was produces, characterized and used to produce L-DOPA. The M36 tyrosinase enzyme showed optimum monophenolase and diphenolase activity at pH 7.5 and conserved its maximum activity over than 95 % at pH ranging from 6.5 to 8.0. The M36 tyrosinase enzyme showed optimum monophenolase and diphenolase activity at 40 °C also, the enzyme conserved 100% of its original activity at 4-45 °C. The M36 tyrosinase enzyme was inhibited strongly by β-mercaptoethanol and about 90% by 5mmol of EDTA (a chelating agent). Although the enzyme was activated at the presence of 1mM SDS, it was strongly inhibited at high concentration of SDS (above 15mM). In TLC analysis, the transformation of L-tyrosine to L-DOPA was conspicuously detected.
机译：酪氨酸酶是一种3型含铜酶，催化L-酪氨酸转化为L-DOPA，最后转化为黑色素。在这项研究中，来自天然巨大芽孢杆菌的酪氨酸酶。产生，表征并用于生产L-DOPA的菌株M36。 M36酪氨酸酶在pH 7.5时表现出最佳的单酚酶和双酚酶活性，并且在6.5至8.0的pH范围内，其最大活性保持超过95％。 M36酪氨酸酶在40°C时也显示出最佳的单酚酶和双酚酶活性，该酶在4-45°C时保留了其原始活性的100％。 M36酪氨酸酶被β-巯基乙醇强烈抑制，约90％被5mmol EDTA（螯合剂）抑制。尽管该酶在1mM SDS存在下被激活，但在高浓度SDS（高于15mM）下却被强烈抑制。在TLC分析中，明显检测到L-酪氨酸向L-DOPA的转化。

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