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首页> 外文期刊>Journal of Proteins and Proteomics >A NEW THERMOPHILIC POLYPHENOL OXIDASE FROM Bacillus sp.: PARTIAL PURIFICATION AND BIOCHEMICAL CHARACTERIZATION
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A NEW THERMOPHILIC POLYPHENOL OXIDASE FROM Bacillus sp.: PARTIAL PURIFICATION AND BIOCHEMICAL CHARACTERIZATION

机译：芽孢杆菌的一种新的热酚氧化酶：部分纯化和生化特性。

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摘要

Polyphenol oxidases (PPOs) catalyze the oxidation of phenolic compounds which makes them highlyuseful biocatalysts for various biotechnological applications. Although they are commonly found in animals,plants and fungi, recent genome analysis have shown that PPOs are also widespread in bacterial species. In thisstudy, detection, partial purification and biochemical characterization of PPO from thermophilic Bacillus sp.,which was isolated from a geothermal region, was achieved. The results of activity staining and activitymeasurements revealed the enzyme was intracellular. Partial purification was performed by acetone precipitation,ion exchange and gel filtration chromatography with 50% yield and 7.32 purification fold. Characterization studiesindicated that the enzyme showed highest activity at pH 7.0 and 60 oC, was stable at temperatures between 30and 60 oC and more than 80% of activity was retained in the pH range of 5-8. The results of effect of metal ionand other reagents on enzyme activity revealed that the enzyme was totally inhibited in the presence of DTTand sodium diethyldithiocarbamate and highly activated with copper ions. Km and Vmax values for the enzymewere determined as 91mM and 2.25 ??abs/min/ml, respectively.
机译：多酚氧化酶（PPO）催化酚类化合物的氧化，这使其成为各种生物技术应用中非常有用的生物催化剂。尽管它们通常在动物，植物和真菌中发现，但最近的基因组分析表明PPO在细菌物种中也很普遍。本研究实现了从地热区分离的嗜热芽孢杆菌的PPO的检测，部分纯化和生物化学表征。活性染色和活性测定的结果表明该酶在细胞内。通过丙酮沉淀，离子交换和凝胶过滤色谱法进行部分纯化，收率50％，纯化倍数为7.32。表征研究表明，该酶在pH 7.0和60 oC时显示最高活性，在30至60 oC的温度下稳定，并且在5-8的pH范围内保留了80％以上的活性。金属离子和其他试剂对酶活性的影响结果表明，在DTT和二乙基二硫代氨基甲酸钠存在下，该酶被完全抑制，并被铜离子高度活化。该酶的Km和Vmax值分别确定为91mM和2.25？abs / min / ml。

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