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Arginine catabolism and acid tolerance response in Lactobacillus reuteri isolated from sourdough

机译：从面团中分离出的罗伊氏乳杆菌的精氨酸分解代谢和耐酸反应

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摘要

The physiological role of arginine degradation by the arginine deiminase (ADI) pathway and its relationship with the acid tolerance response (ATR) in Lactobacillus reuteri CRL 1098 cells, a lactic acid bacterium of sourdough origin, were studied. The activity of the ADI pathway enzymes (ADI, ornithine transcarbamoylase and carbamate kinase) in L. reuteri CRL 1098 grown in presence of arginine and the formation of ammonia (1.39 mmol l~(-1)) and citrulline (1.66 mmol l~(-1)) from arginine catabolism indicated the presence of the ADI pathway in this micro-organism. This system would be involved in the ATR developed by cells grown with arginine and adapted at pH 5.0. The results indicated that the ADI system is triggered either by the adaptation of exponentially growing cells at low pH or by energy depletion of the cells during the stationary phase. Results suggest that ADI is an important component of the ATR observed at pH 5.0 since cells at the exponential phase grown without arginine and further adapted and challenged without this amino acid remained sensitive to acid stress. The findings of this work provide information about the arginine catabolism by L. reuteri, which can contribute to protect this micro-organism in acid environments.
机译：研究了精氨酸脱亚氨酶（ADI）途径对精氨酸的降解的生理作用及其与路氏乳杆菌CRL 1098细胞（一种起源于乳酸的细菌）的耐酸反应（ATR）的关系。在精氨酸存在下生长的罗伊氏乳杆菌CRL 1098中ADI途径酶（ADI，鸟氨酸转氨甲酰酶和氨基甲酸酯激酶）的活性，并形成氨（1.39 mmol l〜（-1））和瓜氨酸（1.66 mmol l〜（精氨酸分解代谢的-1））表明该微生物中存在ADI途径。该系统将参与由精氨酸生长并适应pH 5.0的细胞产生的ATR。结果表明，ADI系统是通过在低pH值下成倍增长的细胞适应或在静止期细胞能量耗尽而触发的。结果表明，ADI是在pH 5.0观察到的ATR的重要组成部分，因为指数期的细胞在没有精氨酸的情况下生长，并且在没有该氨基酸的情况下仍能适应和挑战，而该氨基酸仍对酸胁迫敏感。这项工作的发现提供了有关罗伊氏乳杆菌精氨酸分解代谢的信息，这可以有助于在酸性环境中保护这种微生物。

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