proteomic analysis of lactobacillus casei in response to different phs using two-dimensional electrophoresis and maldi tof mass spectroscopy

Background and objectives: lactobacillus casei, an acid-resistant bacterium, has a protective role against the pathogens. so we aimed to determine the proteome of lactobacillus casei atcc39392 strain in response to different phs of 5 and 7 using proteomic analysis. materials and methods: supernatant and bacterial extraction of lactobacillus casei atcc39392 adapts at phs 5 and 7 were isolated using sodium dodecyl sulfate–polyacrylamide gel and two-dimensional gel electrophoresis. the comparison of results showed that 7 protein spots were seen in ph 5 but not in ph 7. afterward, they were excised and sent for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (maldi-tof ms) to be identified. results: seven different proteins (four secretory and three structural) with different roles in human body health were identified. prescribed proteins include putative cell wall associated hydrolase, glycoside hydrolase, beta-n-acetyl hexosaminidase, histidine kinase, chaperonin, metal dependent hydrolase and lysozyme. conclusion: seven isolated proteins with anti-cancer and digestive impresses are proper subjects in therapy or drug delivery approaches especially oral drug usage for protection against stomach acidic area.