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Applied and Environmental Microbiology
Volumn 80, Issue 15, 2014, Pages 4702-4716
The key to acetate: Metabolic fluxes of acetic acid bacteria under cocoa pulp fermentation-simulating conditions
Author keywords

[No Author keywords available]
Indexed keywords

ACETIC ACID; CARBON; COCOA; ETHANOL; EXPERIMENTS; FERMENTATION; ISOTOPES; LACTIC ACID; METABOLISM; PH; PHYSIOLOGY; VOLATILE FATTY ACIDS; YEAST;
EID: 84904910796     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.01048-14     Document Type: Article
Times cited : (84)
References (73)
  • 1
    • 84986841598 scopus 로고
    • Effect of acetic acid on subcellular structures of cocoa bean cotyledons
    • Biehl B, Passern D, Sagemann W. 1982. Effect of acetic acid on subcellular structures of cocoa bean cotyledons. J. Sci. Food Agric. 33:1101-1109. http://dx.doi.org/10.1002/jsfa.2740331107.
    • (1982) J. Sci. Food Agric. , vol.33 , pp. 1101-1109
    • Biehl, B.1    Passern, D.2    Sagemann, W.3
  • 2
    • 0035146091 scopus 로고    scopus 로고
    • Structural and chemical changes in cocoa (Theobroma cacao L) during fermentation, drying and roasting
    • de Brito ES, García NHP, Gallão MI, Cortelazzo AL, Fevereiro PS, Braga MR. 2001. Structural and chemical changes in cocoa (Theobroma cacao L) during fermentation, drying and roasting. J. Sci. Food Agric. 81:281-288. http://dx.doi.org/10.1002/1097-0010(20010115)81:2 <281::AID-JSFA808>3.0.CO;2-B.
    • (2001) J. Sci. Food Agric. , vol.81 , pp. 281-288
    • de Brito, E.S.1    García, N.H.P.2    Gallão, M.I.3    Cortelazzo, A.L.4    Fevereiro, P.S.5    Braga, M.R.6
  • 3
    • 84982341047 scopus 로고
    • Agents inducing the death of cacao seeds during fermentation
    • Quesnel VC. 1965. Agents inducing the death of cacao seeds during fermentation. J. Sci. Food Agric. 16:441-447. http://dx.doi.org/10.1002/jsfa.2740160804.
    • (1965) J. Sci. Food Agric. , vol.16 , pp. 441-447
    • Quesnel, V.C.1
  • 5
    • 55449091106 scopus 로고    scopus 로고
    • Fermentation of cocoa beans: influence of microbial activities and polyphenol concentrations on the flavour of chocolate
    • Camu N, de Winter T, Addo SK, Takrama JS, Bernaert H, de Vuyst L. 2008. Fermentation of cocoa beans: influence of microbial activities and polyphenol concentrations on the flavour of chocolate. J. Sci. Food Agric. 88:2288-2297. http://dx.doi.org/10.1002/jsfa.3349.
    • (2008) J. Sci. Food Agric. , vol.88 , pp. 2288-2297
    • Camu, N.1    de Winter, T.2    Addo, S.K.3    Takrama, J.S.4    Bernaert, H.5    de Vuyst, L.6
  • 6
    • 4644271406 scopus 로고    scopus 로고
    • The microbiology of cocoa fermentation and its role in chocolate quality
    • Schwan RF, Wheals AE. 2004. The microbiology of cocoa fermentation and its role in chocolate quality. Crit. Rev. Food Sci. Nutr. 44:205-221. http://dx.doi.org/10.1080/10408690490464104.
    • (2004) Crit. Rev. Food Sci. Nutr. , vol.44 , pp. 205-221
    • Schwan, R.F.1    Wheals, A.E.2
  • 7
    • 80053948507 scopus 로고    scopus 로고
    • Assessment of the yeast species composition of cocoa bean fermentations in different cocoa-producing regions using denaturing gradient gel electrophoresis
    • Papalexandratou Z, de Vuyst L. 2011. Assessment of the yeast species composition of cocoa bean fermentations in different cocoa-producing regions using denaturing gradient gel electrophoresis. FEMS Yeast Res. 11:564-574. http://dx.doi.org/10.1111/j.1567-1364.2011.00747.x.
    • (2011) FEMS Yeast Res. , vol.11 , pp. 564-574
    • Papalexandratou, Z.1    de Vuyst, L.2
  • 9
    • 84876729048 scopus 로고    scopus 로고
    • Hanseniaspora opuntiae, Saccharomyces cerevisiae, Lactobacillus fermentum, and Acetobacter pasteurianus predominate during wellperformed Malaysian cocoa bean box fermentations, underlining the importance of these microbial species for a successful cocoa bean fermentation process
    • Papalexandratou Z, Lefeber T, Bahrim B, Lee OS, Daniel H, de Vuyst L. 2013. Hanseniaspora opuntiae, Saccharomyces cerevisiae, Lactobacillus fermentum, and Acetobacter pasteurianus predominate during wellperformed Malaysian cocoa bean box fermentations, underlining the importance of these microbial species for a successful cocoa bean fermentation process. Food Microbiol. 35:73-85. http://dx.doi.org/10.1016/j.fm.2013.02.015.
    • (2013) Food Microbiol. , vol.35 , pp. 73-85
    • Papalexandratou, Z.1    Lefeber, T.2    Bahrim, B.3    Lee, O.S.4    Daniel, H.5    de Vuyst, L.6
  • 10
    • 13244283286 scopus 로고    scopus 로고
    • Occurrence and diversity of yeasts involved in fermentation of West African cocoa beans
    • Jespersen L, Nielsen D, Honholt S, Jakobsen M. 2005. Occurrence and diversity of yeasts involved in fermentation of West African cocoa beans. FEMS Yeast Res. 5:441-453. http://dx.doi.org/10.1016/j.femsyr.2004.11.002.
    • (2005) FEMS Yeast Res. , vol.5 , pp. 441-453
    • Jespersen, L.1    Nielsen, D.2    Honholt, S.3    Jakobsen, M.4
  • 11
    • 84857441039 scopus 로고    scopus 로고
    • On-farm implementation of a starter culture for improved cocoa bean fermentation and its influence on the flavour of chocolates produced thereof
    • Lefeber T, Papalexandratou Z, Gobert W, Camu N, de Vuyst L. 2012. On-farm implementation of a starter culture for improved cocoa bean fermentation and its influence on the flavour of chocolates produced thereof. Food Microbiol. 30:379-392. http://dx.doi.org/10.1016/j.fm.2011.12.021.
    • (2012) Food Microbiol. , vol.30 , pp. 379-392
    • Lefeber, T.1    Papalexandratou, Z.2    Gobert, W.3    Camu, N.4    de Vuyst, L.5
  • 12
    • 78650362870 scopus 로고    scopus 로고
    • Kinetic analysis of strains of lactic acid bacteria and acetic acid bacteria in cocoa pulp simulation media toward development of a starter culture for cocoa bean fermentation
    • Lefeber T, Janssens M, Camu N, de Vuyst L. 2010. Kinetic analysis of strains of lactic acid bacteria and acetic acid bacteria in cocoa pulp simulation media toward development of a starter culture for cocoa bean fermentation. Appl. Environ. Microbiol. 76:7708-7716. http://dx.doi.org/10.1128/AEM.01206-10.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 7708-7716
    • Lefeber, T.1    Janssens, M.2    Camu, N.3    de Vuyst, L.4
  • 13
    • 33947371288 scopus 로고    scopus 로고
    • Dynamics and biodiversity of populations of lactic acid bacteria and acetic acid bacteria involved in spontaneous heap fermentation of cocoa beans in Ghana
    • Camu N, de Winter T, Verbrugghe K, Cleenwerck I, Vandamme P, Takrama JS, Vancanneyt M, de Vuyst L. 2007. Dynamics and biodiversity of populations of lactic acid bacteria and acetic acid bacteria involved in spontaneous heap fermentation of cocoa beans in Ghana. Appl. Environ. Microbiol. 73:1809-1824. http://dx.doi.org/10.1128/AEM.02189-06.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 1809-1824
    • Camu, N.1    de Winter, T.2    Verbrugghe, K.3    Cleenwerck, I.4    Vandamme, P.5    Takrama, J.S.6    Vancanneyt, M.7    de Vuyst, L.8
  • 14
    • 0001835767 scopus 로고
    • The effects of the organic acids in cocoa on the flavour of chocolate
    • Holm CS, Aston JW, Douglas K. 1993. The effects of the organic acids in cocoa on the flavour of chocolate. J. Sci. Food Agric. 61:65-71. http://dx.doi.org/10.1002/jsfa.2740610111.
    • (1993) J. Sci. Food Agric. , vol.61 , pp. 65-71
    • Holm, C.S.1    Aston, J.W.2    Douglas, K.3
  • 15
    • 83155185389 scopus 로고    scopus 로고
    • Species diversity, community dynamics, and metabolite kinetics of the microbiota associated with traditional Ecuadorian spontaneous cocoa bean fermentations
    • Papalexandratou Z, Falony G, Romanens E, Jimenez JC, Amores F, Daniel H, de Vuyst L. 2011. Species diversity, community dynamics, and metabolite kinetics of the microbiota associated with traditional Ecuadorian spontaneous cocoa bean fermentations. Appl. Environ. Microbiol. 77: 7698-7714. http://dx.doi.org/10.1128/AEM.05523-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 7698-7714
    • Papalexandratou, Z.1    Falony, G.2    Romanens, E.3    Jimenez, J.C.4    Amores, F.5    Daniel, H.6    de Vuyst, L.7
  • 16
    • 80051474525 scopus 로고    scopus 로고
    • Spontaneous organic cocoa bean box fermentations in Brazil are characterized by a restricted species diversity of lactic acid bacteria and acetic acid bacteria
    • Papalexandratou Z, Vrancken G, de Bruyne K, Vandamme P, de Vuyst L. 2011. Spontaneous organic cocoa bean box fermentations in Brazil are characterized by a restricted species diversity of lactic acid bacteria and acetic acid bacteria. Food Microbiol. 28:1326-1338. http://dx.doi.org/10.1016/j.fm.2011.06.003.
    • (2011) Food Microbiol. , vol.28 , pp. 1326-1338
    • Papalexandratou, Z.1    Vrancken, G.2    de Bruyne, K.3    Vandamme, P.4    de Vuyst, L.5
  • 17
    • 37849035985 scopus 로고    scopus 로고
    • Influence of turning and environmental contamination on the dynamics of populations of lactic acid and acetic acid bacteria involved in spontaneous cocoa bean heap fermentation in Ghana
    • Camu N, Gonzalez A, de Winter T, van Schoor A, de Bruyne K, Vandamme P, Takrama JS, Addo SK, de Vuyst L. 2008. Influence of turning and environmental contamination on the dynamics of populations of lactic acid and acetic acid bacteria involved in spontaneous cocoa bean heap fermentation in Ghana. Appl. Environ. Microbiol. 74:86-98. http://dx.doi.org/10.1128/AEM.01512-07.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 86-98
    • Camu, N.1    Gonzalez, A.2    de Winter, T.3    van Schoor, A.4    de Bruyne, K.5    Vandamme, P.6    Takrama, J.S.7    Addo, S.K.8    de Vuyst, L.9
  • 18
    • 79952003749 scopus 로고    scopus 로고
    • Dynamics and species diversity of communities of lactic acid bacteria and acetic acid bacteria during spontaneous cocoa bean fermentation in vessels
    • Lefeber T, Gobert W, Vrancken G, Camu N, de Vuyst L. 2011. Dynamics and species diversity of communities of lactic acid bacteria and acetic acid bacteria during spontaneous cocoa bean fermentation in vessels. Food Microbiol. 28:457-464. http://dx.doi.org/10.1016/j.fm.2010.10.010.
    • (2011) Food Microbiol. , vol.28 , pp. 457-464
    • Lefeber, T.1    Gobert, W.2    Vrancken, G.3    Camu, N.4    de Vuyst, L.5
  • 19
    • 77955560347 scopus 로고    scopus 로고
    • Diversity of the total bacterial community associated with Ghanaian and Brazilian cocoa bean fermentation samples as revealed by a 16 S rRNA gene clone library
    • Garcia-Armisen T, Papalexandratou Z, Hendryckx H, Camu N, Vrancken G, Vuyst L, Cornelis P. 2010. Diversity of the total bacterial community associated with Ghanaian and Brazilian cocoa bean fermentation samples as revealed by a 16 S rRNA gene clone library. Appl. Microbiol. Biotechnol. 87:2281-2292. http://dx.doi.org/10.1007/s00253-010-2698-9.
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 2281-2292
    • Garcia-Armisen, T.1    Papalexandratou, Z.2    Hendryckx, H.3    Camu, N.4    Vrancken, G.5    Vuyst, L.6    Cornelis, P.7
  • 20
    • 80052798150 scopus 로고    scopus 로고
    • Interesting starter culture strains for controlled cocoa bean fermentation revealed by simulated cocoa pulp fermentations of cocoa-specific lactic acid bacteria
    • Lefeber T, Janssens M, Moens F, Gobert W, de Vuyst L. 2011. Interesting starter culture strains for controlled cocoa bean fermentation revealed by simulated cocoa pulp fermentations of cocoa-specific lactic acid bacteria. Appl. Environ. Microbiol. 77:6694-6698. http://dx.doi.org/10.1128/AEM.00594-11.
    • (2011) Appl. Environ. Microbiol. , vol.77 , pp. 6694-6698
    • Lefeber, T.1    Janssens, M.2    Moens, F.3    Gobert, W.4    de Vuyst, L.5
  • 21
    • 84880870890 scopus 로고    scopus 로고
    • Complete genome sequence and comparative analysis of Acetobacter pasteurianus 386B, a strain welladapted to the cocoa bean fermentation ecosystem
    • Illeghems K, de Vuyst L, Weckx S. 2013. Complete genome sequence and comparative analysis of Acetobacter pasteurianus 386B, a strain welladapted to the cocoa bean fermentation ecosystem. BMC Genomics 14:526. http://dx.doi.org/10.1186/1471-2164-14-526.
    • (2013) BMC Genomics , vol.14 , pp. 526
    • Illeghems, K.1    de Vuyst, L.2    Weckx, S.3
  • 22
    • 79952253992 scopus 로고    scopus 로고
    • Transcriptome response to different carbon sources in Acetobacter aceti
    • Sakurai K, Arai H, Ishii M, Igarashi Y. 2011. Transcriptome response to different carbon sources in Acetobacter aceti. Microbiology 157:899-910. http://dx.doi.org/10.1099/mic.0.045906-0.
    • (2011) Microbiology , vol.157 , pp. 899-910
    • Sakurai, K.1    Arai, H.2    Ishii, M.3    Igarashi, Y.4
  • 23
    • 84897599554 scopus 로고    scopus 로고
    • Oxidation of metabolites highlights the microbial interactions and role of Acetobacter pasteurianus during cocoa bean fermentation
    • Moens F, Lefeber T, de Vuyst L. 2014. Oxidation of metabolites highlights the microbial interactions and role of Acetobacter pasteurianus during cocoa bean fermentation. Appl. Environ. Microbiol. 80:1848-1857. http://dx.doi.org/10.1128/AEM.03344-13.
    • (2014) Appl. Environ. Microbiol. , vol.80 , pp. 1848-1857
    • Moens, F.1    Lefeber, T.2    de Vuyst, L.3
  • 24
    • 0010426019 scopus 로고
    • Lactate and pyruvate catabolism in acetic acid bacteria
    • de Ley J, Schell J. 1962. Lactate and pyruvate catabolism in acetic acid bacteria. J. Gen. Microbiol. 29:589-601. http://dx.doi.org/10.1099/00221287-29-4-589.
    • (1962) J. Gen. Microbiol. , vol.29 , pp. 589-601
    • de Ley, J.1    Schell, J.2
  • 25
    • 0039290987 scopus 로고
    • On the formation of acetoin by Acetobacter
    • de Ley J. 1959. On the formation of acetoin by Acetobacter. J. Gen. Microbiol. 21:352-365. http://dx.doi.org/10.1099/00221287-21-2-352.
    • (1959) J. Gen. Microbiol. , vol.21 , pp. 352-365
    • de Ley, J.1
  • 26
    • 0035206267 scopus 로고    scopus 로고
    • Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus
    • Chandra Raj K, Ingram L, Maupin-Furlow J. 2001. Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus. Arch. Microbiol. 176:443-451. http://dx.doi.org/10.1007/s002030100348.
    • (2001) Arch. Microbiol. , vol.176 , pp. 443-451
    • Chandra Raj, K.1    Ingram, L.2    Maupin-Furlow, J.3
  • 27
    • 17644375240 scopus 로고    scopus 로고
    • The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria
    • Sauer U, Eikmanns BJ. 2005. The PEP-pyruvate-oxaloacetate node as the switch point for carbon flux distribution in bacteria. FEMS Microbiol. Rev. 29:765-794. http://dx.doi.org/10.1016/j.femsre.2004.11.002.
    • (2005) FEMS Microbiol. Rev. , vol.29 , pp. 765-794
    • Sauer, U.1    Eikmanns, B.J.2
  • 28
    • 78149407462 scopus 로고    scopus 로고
    • Metabolic fluxes and beyond-systems biology understanding and engineering of microbial metabolism
    • Kohlstedt M, Becker J, Wittmann C. 2010. Metabolic fluxes and beyond-systems biology understanding and engineering of microbial metabolism. Appl. Microbiol. Biotechnol. 88:1065-1075. http://dx.doi.org/10.1007/s00253-010-2854-2.
    • (2010) Appl. Microbiol. Biotechnol. , vol.88 , pp. 1065-1075
    • Kohlstedt, M.1    Becker, J.2    Wittmann, C.3
  • 29
    • 0032753923 scopus 로고    scopus 로고
    • Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism
    • Sauer U, Lasko DR, Fiaux J, Hochuli M, Glaser R, Szyperski T, Wüthrich K, Bailey JE. 1999. Metabolic flux ratio analysis of genetic and environmental modulations of Escherichia coli central carbon metabolism. J. Bacteriol. 181:6679-6688.
    • (1999) J. Bacteriol. , vol.181 , pp. 6679-6688
    • Sauer, U.1    Lasko, D.R.2    Fiaux, J.3    Hochuli, M.4    Glaser, R.5    Szyperski, T.6    Wüthrich, K.7    Bailey, J.E.8
  • 30
    • 84884271403 scopus 로고    scopus 로고
    • Core fluxome and metafluxome of lactic acid bacteria under simulated cocoa pulp fermentation conditions
    • Adler P, Bolten CJ, Dohnt K, Hansen CE, Wittmann C. 2013. Core fluxome and metafluxome of lactic acid bacteria under simulated cocoa pulp fermentation conditions. Appl. Environ. Microbiol. 79:5670-5681. http://dx.doi.org/10.1128/AEM.01483-13.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 5670-5681
    • Adler, P.1    Bolten, C.J.2    Dohnt, K.3    Hansen, C.E.4    Wittmann, C.5
  • 31
    • 34547469423 scopus 로고    scopus 로고
    • Acetobacter ghanensis sp. nov., a novel acetic acid bacterium isolated from traditional heap fermentations of Ghanaian cocoa beans
    • Cleenwerck I, Camu N, Engelbeen K, de Winter T, Vandemeulebroecke K, de Vos P, de Vuyst L. 2007. Acetobacter ghanensis sp. nov., a novel acetic acid bacterium isolated from traditional heap fermentations of Ghanaian cocoa beans. Int. J. Syst. Evol. Microbiol. 57:1647-1652. http://dx.doi.org/10.1099/ijs.0.64840-0.
    • (2007) Int. J. Syst. Evol. Microbiol. , vol.57 , pp. 1647-1652
    • Cleenwerck, I.1    Camu, N.2    Engelbeen, K.3    de Winter, T.4    Vandemeulebroecke, K.5    de Vos, P.6    de Vuyst, L.7
  • 33
    • 84873799110 scopus 로고
    • Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli
    • Bertani G. 1951. Studies on lysogenesis. I. The mode of phage liberation by lysogenic Escherichia coli. J. Bacteriol. 62:293-300.
    • (1951) J. Bacteriol. , vol.62 , pp. 293-300
    • Bertani, G.1
  • 34
    • 0037102384 scopus 로고    scopus 로고
    • In vivo analysis of intracellular amino acid labelings by GC/MS
    • Wittmann C, Hans M, Heinzle E. 2002. In vivo analysis of intracellular amino acid labelings by GC/MS. Anal. Biochem. 307:379-382. http://dx.doi.org/10.1016/S0003-2697(02)00030-1.
    • (2002) Anal. Biochem. , vol.307 , pp. 379-382
    • Wittmann, C.1    Hans, M.2    Heinzle, E.3
  • 35
    • 0036013846 scopus 로고    scopus 로고
    • Comparison of methods for extraction, storage, and silylation of pentafluorobenzyl derivatives of carbonyl compounds and multi-functional carbonyl compounds
    • Spaulding R, Charles M. 2002. Comparison of methods for extraction, storage, and silylation of pentafluorobenzyl derivatives of carbonyl compounds and multi-functional carbonyl compounds. Anal. Bioanal. Chem. 372:808-816. http://dx.doi.org/10.1007/s00216-002-1252-8.
    • (2002) Anal. Bioanal. Chem. , vol.372 , pp. 808-816
    • Spaulding, R.1    Charles, M.2
  • 36
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254. http://dx.doi.org/10.1016/0003-2697(76)90527-3.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 37
    • 0027202712 scopus 로고
    • Characterization of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum
    • Jetten MSM, Sinskey AJ. 1993. Characterization of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum. FEMS Microbiol. Lett. 111:183-188. http://dx.doi.org/10.1111/j.1574-6968.1993.tb06383.x.
    • (1993) FEMS Microbiol. Lett. , vol.111 , pp. 183-188
    • Jetten, M.S.M.1    Sinskey, A.J.2
  • 38
    • 0033931565 scopus 로고    scopus 로고
    • Cloning of the malic enzyme gene from Corynebacterium glutamicum and role of the enzyme in lactate metabolism
    • Gourdon P, Baucher M, Lindley ND, Guyonvarch A. 2000. Cloning of the malic enzyme gene from Corynebacterium glutamicum and role of the enzyme in lactate metabolism. Appl. Environ. Microbiol. 66:2981-2987. http://dx.doi.org/10.1128/AEM.66.7.2981-2987.2000.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2981-2987
    • Gourdon, P.1    Baucher, M.2    Lindley, N.D.3    Guyonvarch, A.4
  • 39
    • 73249151004 scopus 로고    scopus 로고
    • Metabolic engineering of the tricarboxylic acid cycle for improved lysine production by Corynebacterium glutamicum
    • Becker J, Klopprogge C, Schröder H, Wittmann C. 2009. Metabolic engineering of the tricarboxylic acid cycle for improved lysine production by Corynebacterium glutamicum. Appl. Environ. Microbiol. 75:7866-7869. http://dx.doi.org/10.1128/AEM.01942-09.
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 7866-7869
    • Becker, J.1    Klopprogge, C.2    Schröder, H.3    Wittmann, C.4
  • 41
    • 0028202832 scopus 로고
    • Respiratory chains and bioenergetics of acetic acid bacteria
    • Rose A, Tempest D (ed). Academic Press, San Diego, CA
    • Matsushita K, Toyama H, Adachi O. 1994. Respiratory chains and bioenergetics of acetic acid bacteria, p 248. In Rose A, Tempest D (ed), Advances in microbial physiology. Academic Press, San Diego, CA.
    • (1994) Advances in microbial physiology , pp. 248
    • Matsushita, K.1    Toyama, H.2    Adachi, O.3
  • 42
    • 0029148093 scopus 로고
    • Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the threecomponent membrane-bound alcohol dehydrogenase from Acetobacter pasteurianus
    • Kondo K, Beppu T, Horinouchi S. 1995. Cloning, sequencing, and characterization of the gene encoding the smallest subunit of the threecomponent membrane-bound alcohol dehydrogenase from Acetobacter pasteurianus. J. Bacteriol. 177:5048-5055.
    • (1995) J. Bacteriol. , vol.177 , pp. 5048-5055
    • Kondo, K.1    Beppu, T.2    Horinouchi, S.3
  • 43
    • 74149094596 scopus 로고    scopus 로고
    • Characterization of thermotolerant Acetobacter pasteurianus strains and their quinoprotein alcohol dehydrogenases
    • Kanchanarach W, Theeragool G, Yakushi T, Toyama H, Adachi O, Matsushita K. 2010. Characterization of thermotolerant Acetobacter pasteurianus strains and their quinoprotein alcohol dehydrogenases. Appl. Microbiol. Biotechnol. 85:741-751. http://dx.doi.org/10.1007/s00253-009-2203-5.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 741-751
    • Kanchanarach, W.1    Theeragool, G.2    Yakushi, T.3    Toyama, H.4    Adachi, O.5    Matsushita, K.6
  • 44
    • 78651420682 scopus 로고    scopus 로고
    • Genomewide phylogenetic analysis of Gluconobacter, Acetobacter, and Gluconacetobacter
    • Matsutani M, Hirakawa H, Yakushi T, Matsushita K. 2011. Genomewide phylogenetic analysis of Gluconobacter, Acetobacter, and Gluconacetobacter. FEMS Microbiol. Lett. 315:122-128. http://dx.doi.org/10.1111/j.1574-6968.2010.02180.x.
    • (2011) FEMS Microbiol. Lett. , vol.315 , pp. 122-128
    • Matsutani, M.1    Hirakawa, H.2    Yakushi, T.3    Matsushita, K.4
  • 45
    • 66949164842 scopus 로고    scopus 로고
    • OpenFLUX: efficient modelling software for 13C-based metabolic flux analysis
    • Quek L, Wittmann C, Nielsen LK, Krömer JO. 2009. OpenFLUX: efficient modelling software for 13C-based metabolic flux analysis. Microb. Cell Fact. 8:25. http://dx.doi.org/10.1186/1475-2859-8-25.
    • (2009) Microb. Cell Fact. , vol.8 , pp. 25
    • Quek, L.1    Wittmann, C.2    Nielsen, L.K.3    Krömer, J.O.4
  • 46
    • 0037145633 scopus 로고    scopus 로고
    • Correcting mass isotopomer distributions for naturally occurring isotopes
    • van Winden WA, Wittmann C, Heinzle E, Heijnen JJ. 2002. Correcting mass isotopomer distributions for naturally occurring isotopes. Biotechnol. Bioeng. 80:477-479. http://dx.doi.org/10.1002/bit.10393.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 477-479
    • van Winden, W.A.1    Wittmann, C.2    Heinzle, E.3    Heijnen, J.J.4
  • 47
    • 84994800753 scopus 로고    scopus 로고
    • Isotopic compositions of the elements 1997
    • Rosman KJR, Taylor PDP. 1998. Isotopic compositions of the elements 1997. Pure Appl. Chem. 70:217-235. http://dx.doi.org/10.1351/pac 199870010217.
    • (1998) Pure Appl. Chem. , vol.70 , pp. 217-235
    • Rosman, K.J.R.1    Taylor, P.D.P.2
  • 48
    • 0036956758 scopus 로고    scopus 로고
    • Genealogy profiling through strain improvement by using metabolic network analysis: metabolic flux genealogy of several generations of lysine-producing corynebacteria
    • Wittmann C, Heinzle E. 2002. Genealogy profiling through strain improvement by using metabolic network analysis: metabolic flux genealogy of several generations of lysine-producing corynebacteria. Appl. Environ. Microbiol. 68:5843-5859. http://dx.doi.org/10.1128/AEM.68.12.5843-5859.2002.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 5843-5859
    • Wittmann, C.1    Heinzle, E.2
  • 49
    • 84904894986 scopus 로고    scopus 로고
    • Metabolic activity profiling by 13C tracer experiments and mass spectrometry in Corynebacterium glutamicum
    • Barredo JL (ed). Humana Press, Totowa, NJ.
    • Wittmann C, Heinzle E. 2005. Metabolic activity profiling by 13C tracer experiments and mass spectrometry in Corynebacterium glutamicum. In Barredo JL (ed), Methods in biotechnology. Humana Press, Totowa, NJ.
    • (2005) Methods in biotechnology
    • Wittmann, C.1    Heinzle, E.2
  • 50
    • 1642374638 scopus 로고    scopus 로고
    • Impact of the cold shock phenomenon on quantification of intracellular metabolites in bacteria
    • Wittmann C, Krömer JO, Kiefer P, Binz T, Heinzle E. 2004. Impact of the cold shock phenomenon on quantification of intracellular metabolites in bacteria. Anal. Biochem. 327:135-139. http://dx.doi.org/10.1016/j.ab.2004.01.002.
    • (2004) Anal. Biochem. , vol.327 , pp. 135-139
    • Wittmann, C.1    Krömer, J.O.2    Kiefer, P.3    Binz, T.4    Heinzle, E.5
  • 51
    • 0347125317 scopus 로고    scopus 로고
    • Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108
    • Chinnawirotpisan P, Theeragool G, Limtong S, Toyama H, Adachi OO, Matsushita K. 2003. Quinoprotein alcohol dehydrogenase is involved in catabolic acetate production, while NAD-dependent alcohol dehydrogenase in ethanol assimilation in Acetobacter pasteurianus SKU1108. J. Biosci. Bioeng. 96:564-571. http://dx.doi.org/10.1016/S1389-1723(04)70150-4.
    • (2003) J. Biosci. Bioeng. , vol.96 , pp. 564-571
    • Chinnawirotpisan, P.1    Theeragool, G.2    Limtong, S.3    Toyama, H.4    Adachi, O.O.5    Matsushita, K.6
  • 53
    • 0030822667 scopus 로고    scopus 로고
    • The low biomass yields of the acetic acid bacterium Acetobacter pasteurianus are due to a low stoichiometry of respiration-coupled proton translocation
    • Luttik M, van Spanning R, Schipper D, van Dijken JP, Pronk JT. 1997. The low biomass yields of the acetic acid bacterium Acetobacter pasteurianus are due to a low stoichiometry of respiration-coupled proton translocation. Appl. Environ. Microbiol. 63:3345-3351.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 3345-3351
    • Luttik, M.1    van Spanning, R.2    Schipper, D.3    van Dijken, J.P.4    Pronk, J.T.5
  • 54
    • 0034969808 scopus 로고    scopus 로고
    • Compartmentation of metabolism within mitochondria and plastids
    • Bowsher CG, Tobin AK. 2001. Compartmentation of metabolism within mitochondria and plastids. J. Exp. Bot. 52:513-527. http://dx.doi.org/10.1093/jexbot/52.356.513.
    • (2001) J. Exp. Bot. , vol.52 , pp. 513-527
    • Bowsher, C.G.1    Tobin, A.K.2
  • 55
    • 0037617724 scopus 로고    scopus 로고
    • Metabolic engineering of Lactobacillus fermentum for production of mannitol and pure L-lactic acid or pyruvate
    • Aarnikunnas J, von Weymarn N, Rönnholm K, Leisola M, Palva A. 2003. Metabolic engineering of Lactobacillus fermentum for production of mannitol and pure L-lactic acid or pyruvate. Biotechnol. Bioeng. 82:653-663. http://dx.doi.org/10.1002/bit.10615.
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 653-663
    • Aarnikunnas, J.1    von Weymarn, N.2    Rönnholm, K.3    Leisola, M.4    Palva, A.5
  • 56
    • 77952890162 scopus 로고    scopus 로고
    • Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology
    • Yakushi T, Matsushita K. 2010. Alcohol dehydrogenase of acetic acid bacteria: structure, mode of action, and applications in biotechnology. Appl. Microbiol. Biotechnol. 86:1257-1265. http://dx.doi.org/10.1007/s00253-010-2529-z.
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1257-1265
    • Yakushi, T.1    Matsushita, K.2
  • 57
    • 0001045654 scopus 로고
    • Purification and properties of particulate alcohol dehydrogenase from Acetobacter aceti
    • Adachi O, Miyagawa E, Shinagawam E, Matsushita K, Ameyana M. 1978. Purification and properties of particulate alcohol dehydrogenase from Acetobacter aceti. Agric. Biol. Chem. 42:2331-2340. http://dx.doi.org/10.1271/bbb1961.42.2331.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 2331-2340
    • Adachi, O.1    Miyagawa, E.2    Shinagawam, E.3    Matsushita, K.4    Ameyana, M.5
  • 58
    • 0018357356 scopus 로고
    • Pyruvate, orthophosphate dikinase from Acetobacter aceti
    • Schwitzguebel J, Ettlinger L. 1979. Pyruvate, orthophosphate dikinase from Acetobacter aceti. Arch. Microbiol. 122:103-108. http://dx.doi.org/10.1007/BF00408052.
    • (1979) Arch. Microbiol. , vol.122 , pp. 103-108
    • Schwitzguebel, J.1    Ettlinger, L.2
  • 59
    • 0015216976 scopus 로고
    • Pyruvate-phosphate dikinase and the control of gluconeogenesis in Acetobacter xylinum
    • Benziman M, Eizen N. 1971. Pyruvate-phosphate dikinase and the control of gluconeogenesis in Acetobacter xylinum. J. Biol. Chem. 246:57-61.
    • (1971) J. Biol. Chem. , vol.246 , pp. 57-61
    • Benziman, M.1    Eizen, N.2
  • 60
    • 0018938082 scopus 로고
    • Oxaloacetate decarboxylase from Acetobacter aceti
    • Schwitzguébel J, Ettlinger L. 1980. Oxaloacetate decarboxylase from Acetobacter aceti. Arch. Microbiol. 124:63-68. http://dx.doi.org/10.1007/BF00407029.
    • (1980) Arch. Microbiol. , vol.124 , pp. 63-68
    • Schwitzguébel, J.1    Ettlinger, L.2
  • 61
    • 0018374756 scopus 로고
    • Phosphoenolpyruvate carboxylase from Acetobacter aceti
    • Schwitzguébel J, Ettlinger L. 1979. Phosphoenolpyruvate carboxylase from Acetobacter aceti. Arch. Microbiol. 122:109-115. http://dx.doi.org/10.1007/BF00408053.
    • (1979) Arch. Microbiol. , vol.122 , pp. 109-115
    • Schwitzguébel, J.1    Ettlinger, L.2
  • 62
    • 0034680782 scopus 로고    scopus 로고
    • In vivo quantification of parallel and bidirectional fluxes in the anaplerosis of Corynebacterium glutamicum
    • Petersen S, Graaf AA de, Eggeling L, Möllney M, Wiechert W, Sahm H. 2000. In vivo quantification of parallel and bidirectional fluxes in the anaplerosis of Corynebacterium glutamicum. J. Biol. Chem. 275:35932-35941. http://dx.doi.org/10.1074/jbc.M908728199.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35932-35941
    • Petersen, S.1    de Graaf, A.A.2    Eggeling, L.3    Möllney, M.4    Wiechert, W.5    Sahm, H.6
  • 63
    • 0035209302 scopus 로고    scopus 로고
    • Bacillus subtilis metabolism and energetics in carbon-limited and excess-carbon chemostat culture
    • Dauner M, Storni T, Sauer U. 2001. Bacillus subtilis metabolism and energetics in carbon-limited and excess-carbon chemostat culture. J. Bacteriol. 183:7308-7317. http://dx.doi.org/10.1128/JB.183.24.7308-7317.2001.
    • (2001) J. Bacteriol. , vol.183 , pp. 7308-7317
    • Dauner, M.1    Storni, T.2    Sauer, U.3
  • 65
    • 0017387401 scopus 로고
    • Pathways of NADPH formation in Escherichia coli
    • Csonka LN, Fraenkel DG. 1977. Pathways of NADPH formation in Escherichia coli. J. Biol. Chem. 252:3382-3391.
    • (1977) J. Biol. Chem. , vol.252 , pp. 3382-3391
    • Csonka, L.N.1    Fraenkel, D.G.2
  • 66
    • 84865040774 scopus 로고    scopus 로고
    • 13C-flux analysis reveals NADPH-balancing transhydrogenation cycles in stationary phase of nitrogen-starving Bacillus subtilis
    • Rühl M, Le Coq D, Aymerich S, Sauer U. 2012. 13C-flux analysis reveals NADPH-balancing transhydrogenation cycles in stationary phase of nitrogen-starving Bacillus subtilis. J. Biol. Chem. 287:27959-27970. http://dx.doi.org/10.1074/jbc.M112.366492.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27959-27970
    • Rühl, M.1    Le Coq, D.2    Aymerich, S.3    Sauer, U.4
  • 67
    • 27744506402 scopus 로고    scopus 로고
    • Amplified expression of fructose 1,6-bisphosphatase in Corynebacterium glutamicum increases in vivo flux through the pentose phosphate pathway and lysine production on different carbon sources
    • Becker J, Klopprogge C, Zelder O, Heinzle E, Wittmann C. 2005. Amplified expression of fructose 1,6-bisphosphatase in Corynebacterium glutamicum increases in vivo flux through the pentose phosphate pathway and lysine production on different carbon sources. Appl. Environ. Microbiol. 71: 8587-8596. http://dx.doi.org/10.1128/AEM.71.12.8587-8596.2005.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 8587-8596
    • Becker, J.1    Klopprogge, C.2    Zelder, O.3    Heinzle, E.4    Wittmann, C.5
  • 69
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • Sauer U, Canonaco F, Heri S, Perrenoud A, Fischer E. 2004. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279:6613-6619. http://dx.doi.org/10.1074/jbc.M311657200.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 70
    • 84985186235 scopus 로고
    • +-dependent aldehyde dehydrogenase from Acetobacter rancens CCM 1774: purification and properties
    • +-dependent aldehyde dehydrogenase from Acetobacter rancens CCM 1774: purification and properties. J. Basic Microbiol. 28:25-33. http://dx.doi.org/10.1002/jobm.3620280105.
    • (1988) J. Basic Microbiol. , vol.28 , pp. 25-33
    • Hommel, R.1    Kurth, J.2    Kleber, H.3
  • 71
    • 0028926047 scopus 로고
    • Energetics of bacterial growth: balance of anabolic and catabolic reactions
    • Russell JB, Cook GM. 1995. Energetics of bacterial growth: balance of anabolic and catabolic reactions. Microbiol. Rev. 59:48-62.
    • (1995) Microbiol. Rev. , vol.59 , pp. 48-62
    • Russell, J.B.1    Cook, G.M.2
  • 72
    • 84892865799 scopus 로고    scopus 로고
    • Yeasts are essential for cocoa bean fermentation
    • Ho VTT, Zhao J, Fleet G. 2014. Yeasts are essential for cocoa bean fermentation. Int. J. Food Microbiol. 174:72-87. http://dx.doi.org/10.1016/j.ijfoodmicro.2013.12.014.
    • (2014) Int. J. Food Microbiol. , vol.174 , pp. 72-87
    • Ho, V.T.T.1    Zhao, J.2    Fleet, G.3
  • 73
    • 0035206267 scopus 로고    scopus 로고
    • Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus
    • Chandra Raj K, Ingram L, Maupin-Furlow J. 2001. Pyruvate decarboxylase: a key enzyme for the oxidative metabolism of lactic acid by Acetobacter pasteurianus. Arch. Microbiol. 176:443-451. http://dx.doi.org/10.1007/s002030100348.
    • (2001) Arch. Microbiol. , vol.176 , pp. 443-451
    • Chandra Raj, K.1    Ingram, L.2    Maupin-Furlow, J.3

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