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首页> 外文期刊>Applied Microbiology >Uncovering the Lactobacillus plantarum WCFS1 Gallate Decarboxylase Involved in Tannin Degradation
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Uncovering the Lactobacillus plantarum WCFS1 Gallate Decarboxylase Involved in Tannin Degradation

机译：揭示涉及单宁降解的植物乳杆菌WCFS1没食子酸酯脱羧酶

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Lactobacillus plantarum is a lactic acid bacterium able to degrade tannins by the subsequent action of tannase and gallate decarboxylase enzymes. The gene encoding tannase had previously been identified, whereas the gene encoding gallate decarboxylase is unknown. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of gallic-acid induced L. plantarum extracts showed a 54-kDa protein which was absent in the uninduced cells. This protein was identified as Lp_2945, putatively annotated UbiD. Homology searches identified ubiD -like genes located within three-gene operons which encoded the three subunits of nonoxidative aromatic acid decarboxylases. L. plantarum is the only bacterium in which the lpdC ( lp_2945 ) gene and the lpdB and lpdD ( lp_0271 and lp_0272 ) genes are separated in the chromosome. Combination of extracts from recombinant Escherichia coli cells expressing the lpdB , lpdC , and lpdC genes demonstrated that LpdC is the only protein required to yield gallate decarboxylase activity. However, the disruption of these genes in L. plantarum revealed that the lpdB and lpdC gene products are essential for gallate decarboxylase activity. Similar to L. plantarum tannase, which exhibited activity only in esters derived from gallic and protocatechuic acids, purified His6-LpdC protein from E. coli showed decarboxylase activity against gallic and protocatechuic acids. In contrast to the tannase activity, gallate decarboxylase activity is widely present among lactic acid bacteria. This study constitutes the first genetic characterization of a gallate decarboxylase enzyme and provides new insights into the role of the different subunits of bacterial nonoxidative aromatic acid decarboxylases.
机译：植物乳杆菌是一种乳酸菌，能够通过鞣酸酶和没食子酸脱羧酶的后续作用降解单宁。先前已经鉴定出编码鞣酸酶的基因，而编码没食子酸脱羧酶的基因是未知的。没食子酸诱导的植物乳杆菌提取物的十二烷基硫酸钠-聚丙烯酰胺钠凝胶电泳（SDS-PAGE）显示出未诱导细胞中不存在的54kDa蛋白。该蛋白被鉴定为Lp_2945，推测为UbiD。同源性搜索确定了位于三基因操纵子内的ubiD样基因，该基因编码非氧化性芳香酸脱羧酶的三个亚基。植物乳杆菌是唯一在染色体中分离lpdC（lp_2945）基因以及lpdB和lpdD（lp_0271和lp_0272）基因的细菌。表达lpdB，lpdC和lpdC基因的重组大肠杆菌细胞提取物的组合证明LpdC是产生没食子酸脱羧酶活性所需的唯一蛋白质。但是，这些基因在植物乳杆菌中的破坏表明，lpdB和lpdC基因产物对于没食子酸脱羧酶活性至关重要。类似于植物乳杆菌鞣酸酶，其仅在源自没食子酸和原儿茶酸的酯中表现出活性，来自大肠杆菌的纯化的His6-LpdC蛋白显示出针对没食子酸和原儿茶酸的脱羧酶活性。与鞣酸酶活性相反，乳酸菌中广泛存在没食子酸脱羧酶活性。这项研究构成了没食子酸脱羧酶的第一个遗传特征，并为细菌非氧化性芳香酸脱羧酶的不同亚基的作用提供了新的见解。

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