A Rivas-Sendra1, J M Landete, C Alcántara, M Zúñiga. 1. Departamento de Biotecnología de Alimentos, Instituto de Agroquímica y Tecnología de Alimentos (IATA), Consejo Superior de Investigaciones Científicas (CSIC), C/Catedrático Agustín Escardino, Paterna, Valencia, Spain.
Abstract
AIMS: To determine the inhibitory effect of phenolic compounds on Lactobacillus casei BL23, the role of two component signal transduction systems (TCS) and the response of Lact. casei BL23 to p-coumaric acid. METHODS AND RESULTS: Growth of Lact. casei BL23 and 17 derivative strains defective in each TCS harboured by this strain in the presence of p-coumaric acid, ferulic acid, caffeic acid or methyl gallate was monitored. Furthermore, changes in the protein content of Lact. casei BL23 when exposed to p-coumaric acid were evaluated by 2D-SDS-PAGE. Eleven proteins differentially expressed in the presence of p-coumaric acid were detected. Six of them could be identified: ClpP and HtrA, involved in protein turnover and folding, acetyl-CoA carboxylase, involved in lipid metabolism, and an arginyl-tRNA synthetase were more abundant, whereas PurL and PurN, involved in purine biosynthesis, were less abundant. CONCLUSIONS: No significant differences were observed between the parental strain and the TCS-defective mutants. p-Coumaric acid elicited a response against membrane and cytoplasmic damages. SIGNIFICANCE AND IMPACT OF THE STUDY: The inhibitory effect of phenolic compounds on Lact. casei BL23 has been determined. For the first time, cytoplasmic proteins presumably involved in the response of Lact. casei BL23 against p-coumaric acid have been identified.
AIMS: To determine the inhibitory effect of phenolic compounds on Lactobacillus casei BL23, the role of two component signal transduction systems (TCS) and the response of Lact. casei BL23 to p-coumaric acid. METHODS AND RESULTS: Growth of Lact. casei BL23 and 17 derivative strains defective in each TCS harboured by this strain in the presence of p-coumaric acid, ferulic acid, caffeic acid or methyl gallate was monitored. Furthermore, changes in the protein content of Lact. casei BL23 when exposed to p-coumaric acid were evaluated by 2D-SDS-PAGE. Eleven proteins differentially expressed in the presence of p-coumaric acid were detected. Six of them could be identified: ClpP and HtrA, involved in protein turnover and folding, acetyl-CoA carboxylase, involved in lipid metabolism, and an arginyl-tRNA synthetase were more abundant, whereas PurL and PurN, involved in purine biosynthesis, were less abundant. CONCLUSIONS: No significant differences were observed between the parental strain and the TCS-defective mutants. p-Coumaric acid elicited a response against membrane and cytoplasmic damages. SIGNIFICANCE AND IMPACT OF THE STUDY: The inhibitory effect of phenolic compounds on Lact. casei BL23 has been determined. For the first time, cytoplasmic proteins presumably involved in the response of Lact. casei BL23 against p-coumaric acid have been identified.
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