Alkali and halide-resistant catalysis by the multipotent oxidase from Marinomonas mediterranea
Alkali and halide-resistant catalysis by the multipotent oxidase from Marinomonas mediterranea
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DOI：
10.1016/j.jbiotec.2005.01.002
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发表时间：
2005-04-20
影响因子：
4.1
通讯作者：
Valderrama, B
中科院分区：
文献类型：
--
作者：
Jimenez-Juarez, N;Roman-Miranda, R;Valderrama, B
由于真菌漆酶对卤化物和碱性条件的固有敏感性，它们的新应用一直被推迟。为了寻找新的酶源，我们对海洋细菌地中海单胞菌的多能多酚氧化酶PPO1进行了评价。在这里，我们报道，与真菌的对应物相比，PPO1在中性pH以上仍然具有功能，对酚类化合物具有高特异性，特别是对甲氧基取代的单酚类和儿茶酚类。这些特性，加上它对氯化物的耐受性（高达1 M）和它在中性pH （0.9 V）下的高氧化还原电位，表明这种酶可能是一个有趣的特定应用的候选者，如酚类化合物和生物燃料电池的安培测定。(c) 2005 Elsevier B.V.版权所有
The incorporation of fungal laccases into novel applications has been delayed mainly due to their intrinsic sensitivity towards halides and alkaline conditions. In order to explore new sources of enzymes we evaluated the multipotent polyphenol oxidase PPO1 from the marine bacterium Marinomonas mediterranea. Here we report that, in contrast to its fungal counterparts, PPO1 remained functional above neutral pH presenting high specificity for phenolic compounds, in particular for methoxyl- substituted mono-phenols and catechols. These properties, in addition to its tolerance towards chloride (up to I M) and its elevated redox potential at neutral pH (0.9 V), suggest this enzyme may be an interesting candidate for specific applications such as the Amperometric determination of phenolic compounds and bio-fuel cells. (c) 2005 Elsevier B.V. All rights reserved.