메뉴 건너뛰기




Volumn 98, Issue 16, 2014, Pages 7039-7050

Characterization of Thermotoga maritima glycerol dehydrogenase for the enzymatic production of dihydroxyacetone

Author keywords

Carboxymethyl NAD; Dihydroxyacetone production; Enzyme immobilization; Kinetics; Stability; Thermotoga maritima glycerol dehydrogenase

Indexed keywords

ARRHENIUS PLOTS; CONVERGENCE OF NUMERICAL METHODS; ELECTROCATALYSIS; ENZYME IMMOBILIZATION; ENZYME KINETICS; SUBSTRATES; SYNTHESIS (CHEMICAL);

EID: 84905976145     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5658-y     Document Type: Article
Times cited : (11)

References (44)
  • 2
    • 28344449827 scopus 로고    scopus 로고
    • Study of the inhibitory effect of the product dihydroxyacetone on Gluconobacter oxydans in a semi-continuous two-stage repeated-fed-batch process
    • DOI 10.1007/s00449-005-0009-0
    • Bauer R, Katsikis N, Varga S, Hekmat D (2005) Study of the inhibitory effect of the product dihydroxyacetone on Gluconobacter oxydans in a semi-continuous two-stage repeated-fed-batch process. Bioproc Biosys Engin 28:37-43 (Pubitemid 41718224)
    • (2005) Bioprocess and Biosystems Engineering , vol.28 , Issue.1 , pp. 37-43
    • Bauer, R.1    Katsikis, N.2    Varga, S.3    Hekmat, D.4
  • 3
    • 84905990317 scopus 로고
    • Sweetener and flavoring compositions and method of producing same
    • US Patent 4,277,511A
    • Bliznak JB, Harcarufka RE (1981) Sweetener and flavoring compositions and method of producing same. US Patent 4,277,511A
    • (1981)
    • Bliznak, J.B.1    Harcarufka, R.E.2
  • 9
    • 15644372444 scopus 로고
    • Substituted 1-(1H-imidazol-4-yl)alkyl-benzamides as anti-ischemics and as α-2-adrenergic receptor agonists
    • US Patent 4,923,865A
    • Cossement E, Geerts JP, Gobert J,Michel P,Wulfert E (1990) Substituted 1-(1H-imidazol-4-yl)alkyl-benzamides as anti-ischemics and as α-2-adrenergic receptor agonists. US Patent 4,923,865A
    • (1990)
    • Cossement, E.1    Geerts, J.P.2    Gobert, J.3    Michel, P.4    Wulfert, E.5
  • 10
    • 0013863538 scopus 로고
    • The interpretation of non-hyperbolic rate curves for two-substrate enzymes
    • Ferdinand W (1966) The interpretation of non-hyperbolic rate curves for two-substrate enzymes. Biochem J 98:278-283
    • (1966) Biochem J , vol.98 , pp. 278-283
    • Ferdinand, W.1
  • 11
    • 13644253751 scopus 로고    scopus 로고
    • 6-linked immobilized cofactors using kinetic-based enzyme capture strategies
    • 6-linked immobilized cofactors using kinetic-based enzyme capture strategies. Anal Biochem 338:102-112
    • (2005) Anal Biochem , vol.338 , pp. 102-112
    • Forde, J.1    Oakey, L.2    Jennings, L.3    Mulchahy, P.4
  • 12
    • 84956498226 scopus 로고
    • Manufacture of 1,2-propylene glycol
    • US Patent 5,306,847A
    • Gehrer E, Wolfgang H (1994) Manufacture of 1,2-propylene glycol. US Patent 5,306,847A
    • (1994)
    • Gehrer, E.1    Wolfgang, H.2
  • 14
    • 0346461714 scopus 로고    scopus 로고
    • Optimization of the microbial synthesis of dihydroxyacetone from glycerol with Gluconobacter oxydans
    • DOI 10.1007/s00449-003-0338-9
    • Hekmat D, Bauer R, Fricke J (2003) Optimization of the microbial synthesis of dihydroxyacetone from glycerol with Gluconobacter oxydans. Bioproc Biosys Engin 26:109-116 (Pubitemid 38082906)
    • (2003) Bioprocess and Biosystems Engineering , vol.26 , Issue.2 , pp. 109-116
    • Hekmat, D.1    Bauer, R.2    Fricke, J.3
  • 15
    • 0019060724 scopus 로고
    • Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments
    • doi:10.1073/pnas.77.9.5055
    • Henis YI, Levitzki A (1980) Mechanism of negative cooperativity in glyceraldehyde-3-phosphate dehydrogenase deduced from ligand competition experiments. Proc Natl Acad Sci U S A 77:5055-5059. doi:10.1073/pnas.77.9.5055
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 5055-5059
    • Henis, Y.I.1    Levitzki, A.2
  • 16
    • 0025368574 scopus 로고
    • Explanation of the non-hyperbolic kinetics of the glutathione S-transferases by the simplest steady-state random sequential Bi Bi mechanism
    • DOI 10.1016/0006-2952(90)90621-Q
    • Ivanetich KM, Goold RD, Sikakana CN (1990) Explanation of the non-hyperbolic kinetics of the glutathione s-transferases by the simplest steady-state random sequential bi bi mechanism. Biochem Pharmicol 39:1999-2004 (Pubitemid 20187338)
    • (1990) Biochemical Pharmacology , vol.39 , Issue.12 , pp. 1999-2004
    • Ivanetich, K.M.1    Goold, R.D.2    Sikakana, C.N.T.3
  • 17
    • 0344931131 scopus 로고
    • Alteration of skin surface protein with dihydroxyacetone: A useful application of the Maillard browning reaction
    • Labuza TP, Reineccius GA, Monnier VM, O'Brien J, Baynes JW (eds) The Royal Society of Chemistry, Cambridge
    • Johnson JA, Fusaro RM (1994) Alteration of skin surface protein with dihydroxyacetone: a useful application of the Maillard browning reaction. In: Labuza TP, Reineccius GA, Monnier VM, O'Brien J, Baynes JW (eds) Maillard Reactions in Chemistry, Food, and Health. The Royal Society of Chemistry, Cambridge, pp 114-119
    • (1994) Maillard Reactions in Chemistry, Food, and Health , pp. 114-119
    • Johnson, J.A.1    Fusaro, R.M.2
  • 18
    • 79953202878 scopus 로고    scopus 로고
    • Simulation of multistep enzyme-catalyzed methanol oxidation in biofuel cells
    • doi:10.1149/1.3561690
    • Kar P, Wen H, Li H, Minteer SD, Calabrese Barton S (2011) Simulation of multistep enzyme-catalyzed methanol oxidation in biofuel cells. J Electrochem Soc 158:B580-B586. doi:10.1149/1.3561690
    • (2011) J Electrochem Soc , vol.158
    • Kar, P.1    Wen, H.2    Li, H.3    Minteer, S.D.4    Calabrese Barton, S.5
  • 19
    • 0037033008 scopus 로고    scopus 로고
    • Proteomics and models for enzyme cooperativity
    • Koshland DE, Hamadani K (2002) Proteomics and models for enzyme cooperativity. J Biol Chem 277:46841-46844
    • (2002) J Biol Chem , vol.277 , pp. 46841-46844
    • Koshland, D.E.1    Hamadani, K.2
  • 20
    • 84863068022 scopus 로고    scopus 로고
    • NADH oxidation by electropolymerized azines on carbon nanotube modified electrodes
    • Li H, Wen H, Calabrese Barton S (2012) NADH oxidation by electropolymerized azines on carbon nanotube modified electrodes. Electroan 24:398-406
    • (2012) Electroan , vol.24 , pp. 398-406
    • Li, H.1    Wen, H.2    Calabrese Barton, S.3
  • 21
    • 77954535362 scopus 로고    scopus 로고
    • Enhanced production of dihydroxyacetone from glycerol by overexpression of glycerol dehydrogenase in an alcohol dehydrogenase-deficient mutant of Gluconobacter oxydans
    • Li M, Wu J, Liu X, Lin J, Wei D, Chen H (2010) Enhanced production of dihydroxyacetone from glycerol by overexpression of glycerol dehydrogenase in an alcohol dehydrogenase-deficient mutant of Gluconobacter oxydans. Bioresour Technol 101:8294-8299
    • (2010) Bioresour Technol , vol.101 , pp. 8294-8299
    • Li, M.1    Wu, J.2    Liu, X.3    Lin, J.4    Wei, D.5    Chen, H.6
  • 22
    • 0015730613 scopus 로고
    • + analogue, its application in affinity chromatography and as a functioning coenzyme
    • + analogue, its application in affinity chromatography and as a functioning coenzyme. Eur J Biochem 40:187-193
    • (1973) Eur J Biochem , vol.40 , pp. 187-193
    • Lindberg, M.1    Larsson, P.2    Mosbach, K.3
  • 23
    • 60849122826 scopus 로고    scopus 로고
    • 1,3-Propanediol dehydrogenase from Klebsiella pneumoniae: Decameric quaternary structure and possible subunit cooperativity
    • doi:10.1128/jb.01077-08
    • Marçal D, Rego AT, Carrondo MA, Enguita FJ (2009) 1,3-Propanediol dehydrogenase from Klebsiella pneumoniae: decameric quaternary structure and possible subunit cooperativity. J Bacteriol 191:1143-1151. doi:10.1128/jb.01077- 08
    • (2009) J Bacteriol , vol.191 , pp. 1143-1151
    • Marçal, D.1    Rego, A.T.2    Carrondo, M.A.3    Enguita, F.J.4
  • 24
    • 0021826470 scopus 로고
    • + 2-oxidoreductase (glycerol dehydrogenase) from Schizosaccharomyces pombe
    • + 2-oxidoreductase (glycerol dehydrogenase) from Schizosaccharomyces pombe. J Gen Microbiol 131:1581-1588
    • (1985) J Gen Microbiol , vol.131 , pp. 1581-1588
    • Marshall, J.H.1    May, J.W.2    Sloan, J.3
  • 25
    • 0016159929 scopus 로고
    • Purification and kinetic characterization of a monovalent cation-activated glycerol dehydrogenase from Aerobacter aerogenes
    • McGregor WG, Phillips JE, Suelter CH (1974) Purification and kinetic characterization of a monovalent cation-activated glycerol dehydrogenase from Aerobacter aerogenes. J Biol Chem 249:3132-3139
    • (1974) J Biol Chem , vol.249 , pp. 3132-3139
    • McGregor, W.G.1    Phillips, J.E.2    Suelter, C.H.3
  • 27
    • 78650339870 scopus 로고
    • Further characterization of glycerol dehydrogenase from Cellulomonas sp. NT3060
    • Nishise H, Nagao A, Tani Y, Yamada H (1984) Further characterization of glycerol dehydrogenase from Cellulomonas sp. NT3060. Agric Biol Chem 48:1603-1609
    • (1984) Agric Biol Chem , vol.48 , pp. 1603-1609
    • Nishise, H.1    Nagao, A.2    Tani, Y.3    Yamada, H.4
  • 28
    • 0033082714 scopus 로고    scopus 로고
    • A kinetic locking-on strategy for bioaffinity purification: Further studies with alcohol dehydrogenase
    • DOI 10.1006/prep.1998.0995
    • O'Flaherty M, McMahon M, Mulcahy P (1999) A kinetic locking-on strategy for bioaffinity purification: further studies with alcohol dehydrogenase. Protein Expr Purif 15:127-145 (Pubitemid 29321479)
    • (1999) Protein Expression and Purification , vol.15 , Issue.1 , pp. 127-145
    • O'Flaherty, M.1    McMahon, M.2    Mulcahy, P.3
  • 29
    • 8844238265 scopus 로고    scopus 로고
    • +
    • DOI 10.1016/j.ab.2004.08.036, PII S0003269704006992
    • Oakey L, Mulcahy P (2004) Immobilized cofactor derivatives for kinetic-based enzyme capture strategies: direct coupling of NAD(P)+. Anal Biochem 335:316-325 (Pubitemid 39535197)
    • (2004) Analytical Biochemistry , vol.335 , Issue.2 , pp. 316-325
    • Oakey, L.1    Mulcahy, P.2
  • 30
    • 84905989517 scopus 로고
    • Substituted 2-mercapto-imidazoles and their preparation
    • US Patent 4,584,383A
    • Parhi SSL (1986) Substituted 2-mercapto-imidazoles and their preparation. US Patent 4,584,383A
    • (1986)
    • Parhi, S.S.L.1
  • 32
    • 0033199021 scopus 로고    scopus 로고
    • Biocatalysis in organic media using enzymes from extremophiles
    • DOI 10.1016/S0141-0229(99)00075-7, PII S0141022999000757
    • Sellek GA, Chaudhuri JB (1999) Biocatalysis in organic media using enzymes from extremophiles. Enzyme Microbial Technol 25:471-482. doi:10.1016/s0141-0229(99)00075-7 (Pubitemid 29408605)
    • (1999) Enzyme and Microbial Technology , vol.25 , Issue.6 , pp. 471-482
    • Sellek, G.A.1    Chaudhuri, J.B.2
  • 37
    • 84905969712 scopus 로고    scopus 로고
    • Production of optically active α-hydroxyacetals
    • European Patent 1,187,798A
    • Studer M (2003) Production of optically active α-hydroxyacetals. European Patent 1,187,798A
    • (2003)
    • Studer, M.1
  • 39
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermophilic enzymes: Sources, uses, and molecular mechanisms for thermostability
    • DOI 10.1128/MMBR.65.1.1-43.2001
    • Vieille C, Zeikus JG (2001) Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol Mol Biol Rev 65:1-43 (Pubitemid 32204286)
    • (2001) Microbiology and Molecular Biology Reviews , vol.65 , Issue.1 , pp. 1-43
    • Vieille, C.1    Zeikus, G.J.2
  • 40
    • 77954251837 scopus 로고    scopus 로고
    • Regeneration of nicotinamide coenzymes: Principles and applications for the synthesis of chiral compounds
    • doi:10.1007/10-2009-55
    • Weckbecker A, Groger H, Hummel W (2010) Regeneration of nicotinamide coenzymes: principles and applications for the synthesis of chiral compounds. Adv Biochem Engin/Biotechnol 120:195-242. doi:10.1007/10-2009-55
    • (2010) Adv Biochem Engin/Biotechnol , vol.120 , pp. 195-242
    • Weckbecker, A.1    Groger, H.2    Hummel, W.3
  • 43
    • 7944232492 scopus 로고    scopus 로고
    • Synthesis of optically active diols by Escherichia coli transformant cells that express the glycerol dehydrogenase gene of Hansenula polymorpha DL-1
    • DOI 10.1002/elsc.200410045
    • Yamada-Onodera K, Kawahara N, Tani Y, YamamotoH (2004) Synthesis of optically active diols by Escherichia coli transformant cells that express the glycerol dehydrogenase gene of Hansenula polymorpha DL-1. Engin Life Sci 4:413-417 (Pubitemid 39467955)
    • (2004) Engineering in Life Sciences , vol.4 , Issue.5 , pp. 413-417
    • Yamada-Onodera, K.1    Kawahara, N.2    Tani, Y.3    Yamamoto, H.4
  • 44
    • 84905975254 scopus 로고    scopus 로고
    • Process for catalytic epoxidation of olefinic compounds, novel cyclic ketone catalysts useful in said process
    • US Patent 5,763,623A
    • Yang D, Zhang JH, Wong MK, Yip YC, Tang MW (1998) Process for catalytic epoxidation of olefinic compounds, novel cyclic ketone catalysts useful in said process. US Patent 5,763,623A
    • (1998)
    • Yang, D.1    Zhang, J.H.2    Wong, M.K.3    Yip, Y.C.4    Tang, M.W.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.