Abstract
Glycerol is one of the most important substrates involved in phospholipid biosynthesis, along with dihydroxyacetone phosphate (DHAP) as an intermediate of glycolysis. Organisms produce glycerol 3-phosphate (G3P) from endogenous DHAP and/or exogenous glycerol to synthesize glycerophospholipids from G3P. On the other hand, organisms can utilize glycerol as a carbon source to generate adenosine triphosphate (ATP). Glycerol metabolism in microorganisms has been investigated for > 50 years. The main research targets have been four bacteria that can utilize glycerol efficiently: Escherichia coli, Enterobacter aerogenes, Klebsiella pneumoniae, and Enterococcus faecalis. E. coli, E. aerogenes, and K. pneumoniae are gram-negative bacteria in the Enterobacteriales order of the class γ-Proteobacteria. In contrast, E. faecalis is a gram-positive bacterium in the Lactobacillales order of the class Bacilli, which are well-known lactic acid bacteria (LAB). Therefore, the glycerol metabolism of E. faecalis is characterized by the properties of both gram-positive bacteria and LAB, which substantially differ from the other three bacteria. As glycerophospholipids are essential for LAB, genes encoding the enzyme for glycerol metabolism (including G3P synthesis) are broadly detected from various LAB. However, these LAB’s classification and trend remained unclear until now, along with each LAB’s ability to utilize glycerol. Hence, the present review summarizes LAB’s glycerol metabolic pathway and regulation mechanism based on the distribution of the genes involved in those and discusses the peculiarities of glycerol metabolism in E. faecalis.
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31 May 2019
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References
Alvarez M de F, Medina R, Pasteris SE, Strasser de Saad AM, Sesma F (2004) Glycerol metabolism of Lactobacillus rhamnosus ATCC 7469: cloning and expression of two glycerol kinase genes. J Mol Microbiol Biotechnol 7:170–181. https://doi.org/10.1159/000079826
Athenstaedt K, Daum G (1999) Phosphatidic acid, a key intermediate in lipid metabolism. Eur J Biochem 266:1–16. https://doi.org/10.1046/j.1432-1327.1999.00822.x
Axelsson L (1998) Lactic acid bacteria: classification and physiology. In: Salminen S, Von Wright A (eds) Lactic acid bacteria: microbiology and functional aspects, 2nd edn. Marcel Dekker, New York, pp 1–72
Bächler C, Schneider P, Bähler P, Lustig A, Erni B (2005) Escherichia coli dihydroxyacetone kinase controls gene expression by binding to transcription factor DhaR. EMBO J 24:283–293. https://doi.org/10.1038/sj.emboj.7600517
Bizzini A, Zhao C, Budin-Verneuil A, Sauvageot N, Giard JC, Auffray Y, Hartke A (2010) Glycerol is metabolized in a complex and strain-dependent manner in Enterococcus faecalis. J Bacteriol 192:779–785. https://doi.org/10.1128/JB.00959-09
Bouvet OM, Lenormand P, Ageron E, Grimont PA (1995) Taxonomic diversity of anaerobic glycerol dissimilation in the Enterobacteriaceae. Res Microbiol 146:279–290. https://doi.org/10.1016/0923-2508(96)81051-5
Claiborne A (1986) Studies on the structure and mechanism of Streptococcus faecium L-alpha-glycerophosphate oxidase. J Biol Chem 261:14398–14407
Charrier V, Buckley E, Parsonage D, Galinier A, Darbon E, Jaquinod M, Forest E, Deutscher J, Claiborne A (1997) Cloning and sequencing of two enterococcal glpK genes and regulation of the encoded glycerol kinases by phosphoenolpyruvate-dependent, phosphotransferase system-catalyzed phosphorylation of a single histidyl residue. J Biol Chem 272:14166–14174. https://doi.org/10.1074/jbc.272.22.14166
Chen Z, Liu D (2016) Toward glycerol biorefinery: metabolic engineering for the production of biofuels and chemicals from glycerol. Biotechnol Biofuels 9:205. https://doi.org/10.1186/s13068-016-0625-8
Christen S, Srinivas A, Bähler P, Zeller A, Pridmore D, Bieniossek C, Baumann U, Erni B (2006) Regulation of the Dha operon of Lactococcus lactis: a deviation from the rule followed by the TetR family of transcription regulators. J Biol Chem 281:23129–23137. https://doi.org/10.1074/jbc.M603486200
Ciriminna R, Della Pina C, Rossi M, Pagliaro M (2014) Understanding the glycerol market. Eur J Lipid Sci Technol 116:1432–1439. https://doi.org/10.1002/ejlt.201400229
Cocaign-Bousquet M, Garrigues C, Loubiere P, Lindley ND (1996) Physiology of pyruvate metabolism in Lactococcus lactis. Antonie Van Leeuwenhoek 70:253–267. https://doi.org/10.1007/BF00395936
Coleman RA, Lee DP (2004) Enzymes of triacylglycerol synthesis and their regulation. Prog Lipid Res 43:134–176. https://doi.org/10.1016/S0163-7827(03)00051-1
Condon S (1987) Responses of lactic acid bacteria to oxygen. FEMS Microbiol Lett 46:269–280. https://doi.org/10.1016/0378-1097(87)90112-1
Daniel R, Boenigk R, Gottschalk G (1995a) Purification of 1,3-propanediol dehydrogenase from Citrobacter freundii and cloning, sequencing, and overexpression of the corresponding gene in Escherichia coli. J Bacteriol 177:2151–2156. https://doi.org/10.1128/jb.177.8.2151-2156.1995
Daniel R, Stuertz K, Gottschalk G (1995b) Biochemical and molecular characterization of the oxidative branch of glycerol utilization by Citrobacter freundii. J Bacteriol 177:4392–4401. https://doi.org/10.1128/jb.177.15.4392-4401.1995
Darbon E, Servant P, Poncet S, Deutscher J (2002) Antitermination by GlpP, catabolite repression via CcpA and inducer exclusion triggered by P-GlpK dephosphorylation control Bacillus subtilis glpFK expression. Mol Microbiol 43:1039–1052. https://doi.org/10.1046/j.1365-2958.2002.02800.x
Deibel RH, Kvetkas MJ (1964) Fumarate reduction and its role in the diversion of glucose fermentation by Streptococcus faecalis. J Bacteriol 88:858–864
Deutscher J, Bauer B, Sauerwald H (1993) Regulation of glycerol metabolism in Enterococcus faecalis by phosphoenolpyruvate-dependent phosphorylation of glycerol kinase catalyzed by enzyme I and HPr of the phosphotransferase system. J Bacteriol 175:3730–3733. https://doi.org/10.1128/jb.175.12.3730-3733.1993
Deutscher J, Sauerwald H (1986) Stimulation of dihydroxyacetone and glycerol kinase activity in Streptococcus faecalis by phosphoenolpyruvate-dependent phosphorylation catalyzed by enzyme I and HPr of the phosphotransferase system. J Bacteriol 166:829–836. https://doi.org/10.1128/jb.166.3.829-836.1986
Dobson R, Gray V, Rumbold K (2012) Microbial utilization of crude glycerol for the production of value-added products. J Ind Microbiol Biotechnol 39:217–226. https://doi.org/10.1007/s10295-011-1038-0
Doi Y (2015) L-lactate production from biodiesel-derived crude glycerol by metabolically engineered Enterococcus faecalis: cytotoxic evaluation of biodiesel waste and development of a glycerol-inducible gene expression system. Appl Environ Microbiol 81:2082–2089. https://doi.org/10.1128/AEM.03418-14
Doi Y (2018) Lactic acid fermentation is the main aerobic metabolic pathway in Enterococcus faecalis metabolizing a high concentration of glycerol. Appl Microbiol Biotechnol 102:10183–10192. https://doi.org/10.1007/s00253-018-9351-4
Doi Y, Ikegami Y (2014) Pyruvate formate-lyase is essential for fumarate-independent anaerobic glycerol utilization in the Enterococcus faecalis strain W11. J Bacteriol 196:2472–2480. https://doi.org/10.1128/JB.01512-14
Escapa IF, del Cerro C, García JL, Prieto MA (2013) The role of GlpR repressor in Pseudomonas putida KT2440 growth and PHA production from glycerol. Environ Microbiol 15:93–110. https://doi.org/10.1111/j.1462-2920.2012.02790.x
Fernández M, Zúñiga M (2006) Amino acid catabolic pathways of lactic acid bacteria. Crit Rev Microbiol 32:155–183. https://doi.org/10.1080/10408410600880643
Fugelsang KC, Edwards CG (2007) Wine microbiology: practical applications and procedures. Springer, New York
Garcia-Alles LF, Siebold C, Nyffeler TL, Flükiger-Brühwiler K, Schneider P, Bürgi HB, Baumann U, Erni B (2004) Phosphoenolpyruvate- and ATP-dependent dihydroxyacetone kinases: covalent substrate-binding and kinetic mechanism. Biochemistry 43:13037–13045. https://doi.org/10.1021/bi048575m
Garlapati VK, Shankar U, Budhiraja A (2015) Bioconversion technologies of crude glycerol to value added industrial products. Biotechnol Rep (Amst) 9:9–14. https://doi.org/10.1016/j.btre.2015.11.002
Garvie EI (1980) Bacterial lactate dehydrogenases. Microbiol Rev 44:106–139
Gibellini F, Smith TK (2010) The Kennedy pathway−de novo synthesis of phosphatidylethanolamine and phosphatidylcholine. IUBMB Life 62:414–428. https://doi.org/10.1002/iub.337
Green J, Paget MS (2004) Bacterial redox sensors. Nat Rev Microbiol 2:954–966. https://doi.org/10.1038/nrmicro1022
Gutknecht R, Beutler R, Garcia-Alles LF, Baumann U, Erni B (2001) The dihydroxyacetone kinase of Escherichia coli utilizes a phosphoprotein instead of ATP as phosphoryl donor. EMBO J 20:2480–2486. https://doi.org/10.1093/emboj/20.10.2480
Heller KB, Lin EC, Wilson TH (1980) Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. J Bacteriol 144:274–278
Houten SM, Wanders RJ (2010) A general introduction to the biochemistry of mitochondrial fatty acid β-oxidation. J Inherit Metab Dis 33:469–477. https://doi.org/10.1007/s10545-010-9061-2
Hugenholtz J (1993) Citrate metabolism in lactic acid bacteria. FEMS Microbiol Rev 12:165–178. https://doi.org/10.1016/0168-6445(93)90062-E
Iqbal J, Hussain MM (2009) Intestinal lipid absorption. Am J Physiol Endocrinol Metab 296:E1183–E1194. https://doi.org/10.1152/ajpendo.90899.2008
Javed S, Azeem F, Hussain S, Rasul I, Siddique MH, Riaz M, Afzal M, Kouser A, Nadeem H (2018) Bacterial lipases: a review on purification and characterization. Prog Biophys Mol Biol 132:23–34. https://doi.org/10.1016/j.pbiomolbio.2017.07.014
Jacobs NJ, VanDemark PJ (1960a) Comparison of the mechanism of glycerol oxidation in aerobically and anaerobically grown Streptococcus faecalis. J Bacteriol 79:532–538
Jacobs NJ, VanDemark PJ (1960b) The purification and properties of the α-glycerophosphate-oxidizing enzyme of Streptococcus faecalis 10C1. Arch Biochem Biophys 88:250–255. https://doi.org/10.1016/0003-9861(60)90230-7
Jiang W, Wang S, Wang Y, Fang B (2016) Key enzymes catalyzing glycerol to 1,3-propanediol. Biotechnol Biofuels 9:57. https://doi.org/10.1186/s13068-016-0473-6
Johnson EA, Burke SK, Forage RG, Lin EC (1984) Purification and properties of dihydroxyacetone kinase from Klebsiella pneumoniae. J Bacteriol 160:55–60
Johnson EA, Lin EC (1987) Klebsiella pneumoniae 1,3-propanediol: NAD+ oxidoreductase. J Bacteriol 169:2050–2554. https://doi.org/10.1128/jb.169.5.2050-2054.1987
Kajfasz JK, Mendoza JE, Gaca AO, Miller JH, Koselny KA, Giambiagi-Demarval M, Wellington M, Abranches J, Lemos JA (2012) The Spx regulator modulates stress responses and virulence in Enterococcus faecalis. Infect Immun 80:2265–2275. https://doi.org/10.1128/IAI.00026-12
Kandler O (1983) Carbohydrate metabolism in lactic acid bacteria. Antonie Van Leeuwenhoek 49:209–224. https://doi.org/10.1007/BF00399499
Koditschek LK, Umbreit WW (1969) α-Glycerophosphate oxidase in Streptococcus faecium F 24. J Bacteriol 98:1063–1068
Larson TJ, Cantwell JS, van Loo-Bhattacharya AT (1992) Interaction at a distance between multiple operators controls the adjacent, divergently transcribed glpTQ-glpACB operons of Escherichia coli K-12. J Biol Chem 267:6114–6121
Leboeuf C, Leblanc L, Auffray Y, Hartke A (2000) Characterization of the ccpA gene of Enterococcus faecalis: identification of starvation-inducible proteins regulated by ccpA. J Bacteriol 182:5799–5806. https://doi.org/10.1128/JB.182.20.5799-5806.2000
Lin EC (1976) Glycerol dissimilation and its regulation in bacteria. Annu Rev Microbiol 30:535–5378. https://doi.org/10.1146/annurev.mi.30.100176.002535
Liu WZ, Faber R, Feese M, Remington SJ, Pettigrew DW (1994) Escherichia coli glycerol kinase: role of a tetramer interface in regulation by fructose 1,6-bisphosphate and phosphotransferase system regulatory protein IIIglc. Biochemistry. 33:10120–10126. https://doi.org/10.1021/bi00199a040
Lindgren V, Rutberg L (1974) Glycerol metabolism in Bacillus subtilis: gene-enzyme relationships. J Bacteriol 119:431–442
Ma F, Hanna MA (1999) Biodiesel production: a review. Bioresour Technol 70:1–15. https://doi.org/10.1016/S0960-8524(99)00025-5
Makarova KS, Koonin EV (2007) Evolutionary genomics of lactic acid bacteria. J Bacteriol 189:1199–1208. https://doi.org/10.1128/JB.01351-06
Marciniak BC, Pabijaniak M, de Jong A, Dűhring R, Seidel G, Hillen W, Kuipers OP (2012) High- and low-affinity cre boxes for CcpA binding in Bacillus subtilis revealed by genome-wide analysis. BMC Genomics 13:401. https://doi.org/10.1186/1471-2164-13-401
Murarka A, Dharmadi Y, Yazdani SS, Gonzalez R (2008) Fermentative utilization of glycerol by Escherichia coli and its implications for the production of fuels and chemicals. Appl Environ Microbiol 74:1124–1135. https://doi.org/10.1128/AEM.02192-07
Nicol RW, Marchand K, Lubitz WD (2012) Bioconversion of crude glycerol by fungi. Appl Microbiol Biotechnol 93:1865–1875. https://doi.org/10.1007/s00253-012-3921-7
Pagliaro M, Rossi M (2008) The future of glycerol. The Royal Society of Chemistry, RCS, UK. https://doi.org/10.1039/9781847558305
Papadimitriou K, Alegría Á, Bron PA, de Angelis M, Gobbetti M, Kleerebezem M, Lemos JA, Linares DM, Ross P, Stanton C, Turroni F, van Sinderen D, Varmanen P, Ventura M, Zúñiga M, Tsakalidou E, Kok J (2016) Stress physiology of lactic acid bacteria. Microbiol Mol Biol Rev 80:837–890. https://doi.org/10.1128/MMBR.00076-15
Pfeiler EA, Klaenhammer TR (2007) The genomics of lactic acid bacteria. Trends Microbiol 15:546–553. https://doi.org/10.1016/j.tim.2007.09.010
Ranganathan SV, Narasimhan SL, Muthukumar K (2008) An overview of enzymatic production of biodiesel. Bioresour Technol 99:3975–3981. https://doi.org/10.1016/j.biortech.2007.04.060
Ravcheev DA, Li X, Latif H, Zengler K, Leyn SA, Korostelev YD, Kazakov AE, Novichkov PS, Osterman AL, Rodionov DA (2012) Transcriptional regulation of central carbon and energy metabolism in bacteria by redox-responsive repressor Rex. J Bacteriol 194:1145–1157. https://doi.org/10.1128/JB.06412-11
Riboulet-Bisson E, Hartke A, Auffray Y, Giard JC (2009) Ers controls glycerol metabolism in Enterococcus faecalis. Curr Microbiol 58:201–204. https://doi.org/10.1007/s00284-008-9308-4
Richey DP, Lin EC (1972) Importance of facilitated diffusion for effective utilization of glycerol by Escherichia coli. J Bacteriol 112:784–790
Rivaldi JD, Sousa Silva M, Duarte LC, Ferreira AE, Cordeiro C, de Almeida Felipe MD, de Ponces Freire A, de Mancilha IM (2013) Metabolism of biodiesel-derived glycerol in probiotic Lactobacillus strains. Appl Microbiol Biotechnol 97:1735–1743. https://doi.org/10.1007/s00253-012-4621-z
Ruch FE, Lengeler J, Lin EC (1974) Regulation of glycerol catabolism in Klebsiella aerogenes. J Bacteriol 119:50–56
Ruch FE, Lin EC (1975) Independent constitutive expression of the aerobic and anaerobic pathways of glycerol catabolism in Klebsiella aerogenes. J Bacteriol 124:348–352
Sakamoto M, Komagata K (1996) Aerobic growth of and activities of NADH oxidase and NADH peroxidase in lactic acid bacteria. J Ferment Bioeng 82:210–216. https://doi.org/10.1111/j.1365-2672.2006.02955.x
Sauer M, Russmayer H, Grabherr R, Peterbauer CK, Marx H (2017) The efficient clade: lactic acid bacteria for industrial chemical production. Trends Biotechnol 35:756–769. https://doi.org/10.1016/j.tibtech.2017.05.002
Sauvageot N, Ladjouzi R, Benachour A, Rincé A, Deutscher J, Hartke A (2012) Aerobic glycerol dissimilation via the Enterococcus faecalis DhaK pathway depends on NADH oxidase and a phosphotransfer reaction from PEP to DhaK via EIIADha. Microbiology 158:2661–2666. https://doi.org/10.1099/mic.0.061663-0
Schryvers A, Lohmeier E, Weiner JH (1978) Chemical and functional properties of the native and reconstituted forms of the membrane-bound, aerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. J Biol Chem 253(3):783–788
Schweizer H, Boos W, Larson TJ (1985) Repressor for the sn-glycerol-3-phosphate regulon of Escherichia coli K-12: cloning of the glpR gene and identification of its product. J Bacteriol 161:563–566
Schweizer HP, Po C (1996) Regulation of glycerol metabolism in Pseudomonas aeruginosa: characterization of the glpR repressor gene. J Bacteriol 178:5215–5221. https://doi.org/10.1128/jb.178.17.5215-5221.1996
Schweiger M, Schreiber R, Haemmerle G, Lass A, Fledelius C, Jacobsen P, Tornqvist H, Zechner R, Zimmermann R (2006) Adipose triglyceride lipase and hormone-sensitive lipase are the major enzymes in adipose tissue triacylglycerol catabolism. J Biol Chem 281:40236–40241. https://doi.org/10.1074/jbc.M608048200
Schütz H, Radler F (1984a) Anaerobic reduction of glycerol to propanediol-1.3 by Lactobacillus brevis and Lactobacillus buchneri. Syst Appl Microbiol 5:169–178. https://doi.org/10.1016/S0723-2020(84)80018-1
Schütz H, Radler F (1984b) Propanediol-1,2-dehydratase and metabolism of glycerol of Lactobacillus brevis. Arch Microbiol 139:366–370. https://doi.org/10.1007/BF00408381
Sriramulu DD, Liang M, Hernandez-Romero D, Raux-Deery E, Lünsdorf H, Parsons JB, Warren MJ, Prentice MB (2008) Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation. J Bacteriol 190:4559–4567. https://doi.org/10.1128/JB.01535-07
Strittmatter CF (1959) Flavin-linked oxidative enzymes of Lactobacillus casei. J Biol Chem 234:2794–2800
Subedi KP, Kim I, Kim J, Min B, Park C (2008) Role of GldA in dihydroxyacetone and methylglyoxal metabolism of Escherichia coli K12. FEMS Microbiol Lett 279:180–187. https://doi.org/10.1111/j.1574-6968.2007.01032.x
Sweet G, Gandor C, Voegele R, Wittekindt N, Beuerle J, Truniger V, Lin EC, Boos W (1990) Glycerol facilitator of Escherichia coli: cloning of glpF and identification of the glpF product. J Bacteriol 172:424–430. https://doi.org/10.1128/jb.172.1.424-430.1990
Talarico TL, Axelsson LT, Novotny J, Fiuzat M, Dobrogosz WJ (1990) Utilization of glycerol as a hydrogen acceptor by Lactobacillus reuteri: purification of 1,3-propanediol: NAD oxidoreductase. Appl Environ Microbiol 56:943–948
Talarico TL, Dobrogosz WJ (1990) Purification and characterization of glycerol dehydratase from Lactobacillus reuteri. Appl Environ Microbiol 56:1195–1197
Toraya T, Kuno S, Fukui S (1980) Distribution of coenzyme B12-dependent diol dehydratase and glycerol dehydratase in selected genera of Enterobacteriaceae and Propionibacteriaceae. J Bacteriol 141:1439–1442
Van Gerpen J (2005) Biodiesel processing and production. Fuel Process Technol 86:1097–1107. https://doi.org/10.1016/j.fuproc.2004.11.005
Varga ME, Weiner JH (1995) Physiological role of GlpB of anaerobic glycerol-3-phosphate dehydrogenase of Escherichia coli. Biochem Cell Biol 73:147–153. https://doi.org/10.1139/o95-018
Verneuil N, Rincé A, Sanguinetti M, Posteraro B, Fadda G, Auffray Y, Hartke A, Giard JC (2005a) Contribution of a PerR-like regulator to the oxidative-stress response and virulence of Enterococcus faecalis. Microbiology 151:3997–4004. https://doi.org/10.1099/mic.0.28325-0
Verneuil N, Rincé A, Sanguinetti M, Auffray Y, Hartke A, Giard JC (2005b) Implication of hypR in the virulence and oxidative stress response of Enterococcus faecalis. FEMS Microbiol Lett 252:137–141. https://doi.org/10.1016/j.femsle.2005.08.043
Vesić D, Kristich CJ (2013) A Rex family transcriptional repressor influences H2O2 accumulation by Enterococcus faecalis. J Bacteriol 195:1815–1824. https://doi.org/10.1128/JB.02135-12
Wang Q, Ingram LO, Shanmugam KT (2011) Evolution of D-lactate dehydrogenase activity from glycerol dehydrogenase and its utility for D-lactate production from lignocellulose. Proc Natl Acad Sci U S A 108:18920–18925. https://doi.org/10.1073/pnas.1111085108
Wang ZX, Zhuge J, Fang H, Prior BA (2001) Glycerol production by microbial fermentation: a review. Biotechnol Adv 19:201–223. https://doi.org/10.1016/S0734-9750(01)00060-X
Warner JB, Lolkema JS (2003) CcpA-dependent carbon catabolite repression in bacteria. Microbiol Mol Biol Rev 67:475–490. https://doi.org/10.1128/MMBR.67.4.475-490.2003
Weissenborn DL, Wittekindt N, Larson TJ (1992) Structure and regulation of the glpFK operon encoding glycerol diffusion facilitator and glycerol kinase of Escherichia coli K-12. J Biol Chem 267(9):6122–6131
Whittenbury R (1964) Hydrogen peroxide formation and catalase activity in the lactic acid bacteria. J Gen Microbiol 35:13–26. https://doi.org/10.1099/00221287-35-1-13
Yao J, Rock CO (2013) Phosphatidic acid synthesis in bacteria. Biochim Biophys Acta 1831:495–502. https://doi.org/10.1016/j.bbalip.2012.08.018
Yeh JI, Chinte U, Du S (2008) Structure of glycerol-3-phosphate dehydrogenase, an essential monotopic membrane enzyme involved in respiration and metabolism. Proc Natl Acad Sci U S A 105:3280–3285. https://doi.org/10.1073/pnas.0712331105
Zaunmüller T, Eichert M, Richter H, Unden G (2006) Variations in the energy metabolism of biotechnologically relevant heterofermentative lactic acid bacteria during growth on sugars and organic acids. Appl Microbiol Biotechnol 72:421–429. https://doi.org/10.1007/s00253-006-0514-3
Zielińska K, Fabiszewska A, Świątek M, Szymanowska-Powałowska D (2017) Evaluation of the ability to metabolize 1,2-propanediol by heterofermentative bacteria of the genus Lactobacillus. Electron J Biotechnol 26:60–63. https://doi.org/10.1016/j.ejbt.2017.01.002
Zhang YM, Rock CO (2008) Membrane lipid homeostasis in bacteria. Nat Rev Microbiol 6:222–233. https://doi.org/10.1038/nrmicro1839
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Doi, Y. Glycerol metabolism and its regulation in lactic acid bacteria. Appl Microbiol Biotechnol 103, 5079–5093 (2019). https://doi.org/10.1007/s00253-019-09830-y
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DOI: https://doi.org/10.1007/s00253-019-09830-y