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Volumn 102, Issue 2, 2011, Pages 1837-1843

Simultaneous production of 1,3-dihydroxyacetone and xylitol from glycerol and xylose using a nanoparticle-supported multi-enzyme system with in situ cofactor regeneration

Author keywords

Biosynthesis; Cofactor regeneration; Enzymatic biocatalysis; Glycerol dehydrogenase; Xylose reductase

Indexed keywords

COFACTOR REGENERATION; COFACTORS; DIHYDROXYACETONE; ENZYMATIC BIOCATALYSIS; ENZYME SYSTEMS; GLYCEROL DEHYDROGENASE; IN-SITU; NATIVE ENZYMES; REGENERATION CYCLES; SYNTHETIC REACTIONS; TOTAL TURNOVER; VALUE ADDED PRODUCTS; XYLOSE REDUCTASE;

EID: 78650681129     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2010.09.069     Document Type: Article
Times cited : (79)

References (30)
  • 1
    • 36649017886 scopus 로고    scopus 로고
    • Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes
    • Asuri P., Bale S.S., Pangule R.C., Shah D.A., Kane R.S., Dordick J.S. Structure, function, and stability of enzymes covalently attached to single-walled carbon nanotubes. Langmuir 2007, 23:12318-12321.
    • (2007) Langmuir , vol.23 , pp. 12318-12321
    • Asuri, P.1    Bale, S.S.2    Pangule, R.C.3    Shah, D.A.4    Kane, R.S.5    Dordick, J.S.6
  • 3
    • 35148846126 scopus 로고    scopus 로고
    • A laboratory study of producing docosahexaenoic acid from biodiesel-waste glycerol by microalgal fermentation
    • Chi Z., Pyle D., Wen Z., Frear C., Chen S. A laboratory study of producing docosahexaenoic acid from biodiesel-waste glycerol by microalgal fermentation. Process Biochem. 2007, 42:1537-1545.
    • (2007) Process Biochem. , vol.42 , pp. 1537-1545
    • Chi, Z.1    Pyle, D.2    Wen, Z.3    Frear, C.4    Chen, S.5
  • 4
    • 3042828485 scopus 로고    scopus 로고
    • Enabling multi-enzyme biocatalysis using nanoporous materials
    • El-Zahab B., Jia H., Wang P. Enabling multi-enzyme biocatalysis using nanoporous materials. Biotechnol. Bioeng. 2004, 87:178-183.
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 178-183
    • El-Zahab, B.1    Jia, H.2    Wang, P.3
  • 5
    • 14844336872 scopus 로고    scopus 로고
    • The dihydroxyacetone unit-a versatile C3 building block in organic synthesis
    • Enders D., Voith M., Lenzen A. The dihydroxyacetone unit-a versatile C3 building block in organic synthesis. Angew. Chem. Int. Ed. 2005, 44:1304-1325.
    • (2005) Angew. Chem. Int. Ed. , vol.44 , pp. 1304-1325
    • Enders, D.1    Voith, M.2    Lenzen, A.3
  • 6
    • 0033485581 scopus 로고    scopus 로고
    • Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments
    • Hummel W. Large-scale applications of NAD(P)-dependent oxidoreductases: recent developments. Trends Biotechnol. 1999, 17:487-492.
    • (1999) Trends Biotechnol. , vol.17 , pp. 487-492
    • Hummel, W.1
  • 7
    • 0142073274 scopus 로고    scopus 로고
    • Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility
    • Jia H., Zhu G., Wang P. Catalytic behaviors of enzymes attached to nanoparticles: the effect of particle mobility. Biotechnol. Bioeng. 2003, 84:406-414.
    • (2003) Biotechnol. Bioeng. , vol.84 , pp. 406-414
    • Jia, H.1    Zhu, G.2    Wang, P.3
  • 8
    • 0036752497 scopus 로고    scopus 로고
    • Enzyme-carrying polymeric nanofibers prepared via electrospinning for use as unique biocatalysts
    • Jia H., Zhu G., Vugrinovich B., Kataphinan W., Reneker D.H., Wang P. Enzyme-carrying polymeric nanofibers prepared via electrospinning for use as unique biocatalysts. Biotechnol. Progr. 2002, 18:1027-1032.
    • (2002) Biotechnol. Progr. , vol.18 , pp. 1027-1032
    • Jia, H.1    Zhu, G.2    Vugrinovich, B.3    Kataphinan, W.4    Reneker, D.H.5    Wang, P.6
  • 9
    • 33845964503 scopus 로고    scopus 로고
    • Efficient regeneration of NADPH using an engineered phosphite dehydrogenase
    • Johannes T.W., Woodyer R.D., Zhao H. Efficient regeneration of NADPH using an engineered phosphite dehydrogenase. Biotechnol. Bioeng. 2007, 96:18-26.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 18-26
    • Johannes, T.W.1    Woodyer, R.D.2    Zhao, H.3
  • 10
    • 0141684517 scopus 로고    scopus 로고
    • Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network
    • Kim J., Grate J.W. Single-enzyme nanoparticles armored by a nanometer-scale organic/inorganic network. Nano Lett. 2003, 3:1219-1222.
    • (2003) Nano Lett. , vol.3 , pp. 1219-1222
    • Kim, J.1    Grate, J.W.2
  • 11
    • 27844518415 scopus 로고    scopus 로고
    • Nanostructures for enzyme stabilization
    • Kim J., Grate J.W., Wang P. Nanostructures for enzyme stabilization. Chem. Eng. Sci. 2006, 61:1017-1026.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 1017-1026
    • Kim, J.1    Grate, J.W.2    Wang, P.3
  • 13
    • 0035843122 scopus 로고    scopus 로고
    • Enzymes for chemical synthesis
    • Koeller K.M., Wong C. Enzymes for chemical synthesis. Nature 2001, 409:232-240.
    • (2001) Nature , vol.409 , pp. 232-240
    • Koeller, K.M.1    Wong, C.2
  • 14
    • 0001275962 scopus 로고
    • Preparation of optically active 1,2-diols and α-hydroxy ketones using glycerol dehydrogenase as catalyst: limits to enzyme-catalyzed synthesis due to noncompetitive and mixed inhibition by product
    • Lee L.G., Whitesides G.M. Preparation of optically active 1,2-diols and α-hydroxy ketones using glycerol dehydrogenase as catalyst: limits to enzyme-catalyzed synthesis due to noncompetitive and mixed inhibition by product. J. Org. Chem. 1986, 51:25-36.
    • (1986) J. Org. Chem. , vol.51 , pp. 25-36
    • Lee, L.G.1    Whitesides, G.M.2
  • 15
    • 0028598706 scopus 로고
    • Isotopic analysis of the reaction catalyzed by glycerol dehydrogenase
    • Leichus B.N., Blanchard J.S. Isotopic analysis of the reaction catalyzed by glycerol dehydrogenase. Biochemistry 1994, 33:14642-14649.
    • (1994) Biochemistry , vol.33 , pp. 14642-14649
    • Leichus, B.N.1    Blanchard, J.S.2
  • 16
    • 0026475638 scopus 로고
    • Dihydroxyacetone-containing sunless or self-tanning lotions
    • Levy S.B. Dihydroxyacetone-containing sunless or self-tanning lotions. J. Am. Acad. Dermatol. 1992, 27:989-993.
    • (1992) J. Am. Acad. Dermatol. , vol.27 , pp. 989-993
    • Levy, S.B.1
  • 17
    • 57549094438 scopus 로고    scopus 로고
    • Nanoparticle-supported multi-enzyme biocatalysis with in situ cofactor regeneration
    • Liu W., Zhang S., Wang P. Nanoparticle-supported multi-enzyme biocatalysis with in situ cofactor regeneration. J. Biotechnol. 2009, 139:102-107.
    • (2009) J. Biotechnol. , vol.139 , pp. 102-107
    • Liu, W.1    Zhang, S.2    Wang, P.3
  • 18
    • 34247637888 scopus 로고    scopus 로고
    • Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure
    • Nair S., Kim J., Crawford B., Kim S.H. Improving biocatalytic activity of enzyme-loaded nanofibers by dispersing entangled nanofiber structure. Biomacromolecules 2007, 8:1266-1270.
    • (2007) Biomacromolecules , vol.8 , pp. 1266-1270
    • Nair, S.1    Kim, J.2    Crawford, B.3    Kim, S.H.4
  • 19
    • 0030571272 scopus 로고    scopus 로고
    • Continuous enzymatic production of xylitol with simultaneous coenzyme regeneration in a charged membrane reactor
    • Nidetzky B., Neuhauser W., Haltrich D., Kulbe K.D. Continuous enzymatic production of xylitol with simultaneous coenzyme regeneration in a charged membrane reactor. Biotechnol. Bioeng. 1996, 52:387-396.
    • (1996) Biotechnol. Bioeng. , vol.52 , pp. 387-396
    • Nidetzky, B.1    Neuhauser, W.2    Haltrich, D.3    Kulbe, K.D.4
  • 20
    • 78650339870 scopus 로고
    • Further characterization of glycerol dehydrogenase from Cellulomonas sp. NT3060
    • Nishise H., Nagao A., Tani Y., Yamada H. Further characterization of glycerol dehydrogenase from Cellulomonas sp. NT3060. Agric. Biol. Chem. 1984, 48:1603-1609.
    • (1984) Agric. Biol. Chem. , vol.48 , pp. 1603-1609
    • Nishise, H.1    Nagao, A.2    Tani, Y.3    Yamada, H.4
  • 25
    • 0036740471 scopus 로고    scopus 로고
    • Medical pearl: DHA application for camouflaging segmental vitiligo and piebald lesions
    • Suga Y., Ikejima A., Matsuba S., Ogawa H. Medical pearl: DHA application for camouflaging segmental vitiligo and piebald lesions. J. Am. Acad. Dermatol. 2002, 47:436-438.
    • (2002) J. Am. Acad. Dermatol. , vol.47 , pp. 436-438
    • Suga, Y.1    Ikejima, A.2    Matsuba, S.3    Ogawa, H.4
  • 26
    • 4043075579 scopus 로고    scopus 로고
    • Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme
    • Vertegel A.A., Siegel R.W., Dordick J.S. Silica nanoparticle size influences the structure and enzymatic activity of adsorbed lysozyme. Langmuir 2004, 20:6800-6807.
    • (2004) Langmuir , vol.20 , pp. 6800-6807
    • Vertegel, A.A.1    Siegel, R.W.2    Dordick, J.S.3
  • 27
    • 33751256536 scopus 로고    scopus 로고
    • Nanoscale biocatalyst systems
    • Wang P. Nanoscale biocatalyst systems. Curr. Opin. Biotechnol. 2006, 17:574-579.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 574-579
    • Wang, P.1
  • 28
    • 84941889613 scopus 로고
    • Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration
    • Wichmann R., Wandrey C. Continuous enzymatic transformation in an enzyme membrane reactor with simultaneous NAD(H) regeneration. Biotechnol. Bioeng. 1981, 23:2789-2802.
    • (1981) Biotechnol. Bioeng. , vol.23 , pp. 2789-2802
    • Wichmann, R.1    Wandrey, C.2
  • 29
  • 30
    • 33748082007 scopus 로고    scopus 로고
    • Encapsulation of single enzyme in nanogel with enhanced biocatalytic activity and stability
    • Yan M., Ge J., Liu Z., Ouyang P. Encapsulation of single enzyme in nanogel with enhanced biocatalytic activity and stability. J. Am. Chem. Soc. 2006, 128:11008-11009.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11008-11009
    • Yan, M.1    Ge, J.2    Liu, Z.3    Ouyang, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.