Understanding of how Propionibacterium acidipropionici respond to propionic acid stress at the level of proteomics.
Propionic acid (PA) is an important platform chemical in the food, agriculture, and pharmaceutical industries and is mainly biosynthesized by propionibacteria. Acid tolerance in PA-producing strains is crucial. In previous work, we investigated the acid tolerance mechanism of Propionibacterium acidipropionici at microenvironmental levels by analyzing physiological changes in the parental strain and three PA-tolerant mutants obtained by genome shuffling. However, the molecular mechanism of PA tolerance in P. acidipropionici remained unclear. Here, we performed a comparative proteomics study of P. acidipropionici CGMCC 1.2230 and the acid-tolerant mutant P. acidipropionici WSH1105; MALDI-TOF/MS identified 24 proteins that significantly differed between the parental and shuffled strains. The differentially expressed proteins were mainly categorized as key components of crucial biological processes and the acid stress response. Quantitative reverse transcriptase polymerase chain reaction (qRT-PCR) was used to confirm differential expression of nine key proteins. Overexpression of the secretory protein glyceraldehyde-3-phosphate dehydrogenase and ATP synthase subunit α in Escherichia coli BL21 improved PA and acetic acid tolerance; overexpression of NADH dehydrogenase and methylmalonyl-CoA epimerase improved PA tolerance. These results provide new insights into the acid tolerance of P. acidipropionici and will facilitate the development of PA production through fermentation by propionibacteria.
1] Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China [2] Key Laboratory of Industrial Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China.
Ningzi
N
Guan
School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta 30332, USA.
Hyun-dong
HD
Shin
School of Chemical and Biomolecular Engineering, Georgia Institute of Technology, Atlanta 30332, USA.
Rachel R
RR
Chen
1] Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China [2] Synergetic Innovation Center Of Food Safety and Nutrition, Wuxi 214122, China.
Jianghua
J
Li
1] Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, Jiangnan University, Wuxi 214122, China [2] Synergetic Innovation Center Of Food Safety and Nutrition, Wuxi 214122, China.
Long
L
Liu
Synergetic Innovation Center Of Food Safety and Nutrition, Wuxi 214122, China.
Guocheng
G
Du
Synergetic Innovation Center Of Food Safety and Nutrition, Wuxi 214122, China.
Jian
J
Chen
D019342:Acetic Acid / Q000378:metabolism; D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000235:genetics* / Q000378:metabolism; D025243:Bacterial Proton-Translocating ATPases / Q000235:genetics / Q000378:metabolism; D032621:DNA Shuffling / Q000379:methods*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism; D005285:Fermentation; D015964:Gene Expression Regulation, Bacterial; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating) / Q000235:genetics / Q000378:metabolism; D009245:NADH Dehydrogenase / Q000235:genetics / Q000378:metabolism; D011422:Propionates / Q000378:metabolism*; D011424:Propionibacterium / Q000235:genetics* / Q000378:metabolism; D040901:Proteomics; D019998:Racemases and Epimerases / Q000235:genetics / Q000378:metabolism; D013312:Stress, Physiological; D019076:Transgenes
D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011422:Propionates; D024581:Glyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating); D009245:NADH Dehydrogenase; D025243:Bacterial Proton-Translocating ATPases; D019998:Racemases and Epimerases; C021581:methylmalonyl-coenzyme A racemase; C074428:atpB protein, E coli; C029658:propionic acid; D019342:Acetic Acid