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Volumn 19, Issue 6, 2003, Pages 1643-1647

Continuous D-Tagatose Production by Immobilized Thermostable L-Arabinose Isomerase in a Packed-Bed Bioreactor

Author keywords

[No Author keywords available]

Indexed keywords

BIOREACTORS; ENZYME IMMOBILIZATION; SUBSTRATES;

EID: 0346783288     PISSN: 87567938     EISSN: None     Source Type: Journal    
DOI: 10.1021/bp0340739     Document Type: Article
Times cited : (42)

References (21)
  • 1
    • 0347254772 scopus 로고    scopus 로고
    • Functional sugar substitutes with reduced calories. EP 341062, 1989
    • Marzur, A. W. Functional sugar substitutes with reduced calories. EP 341062, 1989.
    • Marzur, A.W.1
  • 2
    • 0029989031 scopus 로고    scopus 로고
    • D-Tagatose is a bulk sweetener with zero energy determined in rats
    • Livesey, G.; Brown, J. C. D-Tagatose is a bulk sweetener with zero energy determined in rats. J. Nutr. 1996, 126, 1601-1609.
    • (1996) J. Nutr. , vol.126 , pp. 1601-1609
    • Livesey, G.1    Brown, J.C.2
  • 3
    • 0028839816 scopus 로고
    • Sugar substitutes: Their energy values, bulk characteristics, and potential health benefits
    • Levin, G. V.; Zehner, L. R.; Saunder, J. P.; Beadle, J. R. Sugar substitutes: their energy values, bulk characteristics, and potential health benefits. Am. J. Clin. Nutr. 1995, 62, 1161-1168.
    • (1995) Am. J. Clin. Nutr. , vol.62 , pp. 1161-1168
    • Levin, G.V.1    Zehner, L.R.2    Saunder, J.P.3    Beadle, J.R.4
  • 4
    • 0346624869 scopus 로고    scopus 로고
    • Process for manufacturing D-tagatose. U. S. Patent 6,057,135, 2000
    • Ibrahim, O. O.; Spradlin, J. E. Process for manufacturing D-tagatose. U. S. Patent 6,057,135, 2000.
    • Ibrahim, O.O.1    Spradlin, J.E.2
  • 5
  • 6
    • 0031843502 scopus 로고    scopus 로고
    • Optimization of culture conditions for D-tagatose production from D-galactose by Enterobacter agglomerans
    • Oh, D. K.; Roh, H. J.; Kim, S. Y.; Noh, B. S. Optimization of culture conditions for D-tagatose production from D-galactose by Enterobacter agglomerans. Kor. J. Appl. Microbiol. Biotechnol. 1998, 26, 250-256.
    • (1998) Kor. J. Appl. Microbiol. Biotechnol. , vol.26 , pp. 250-256
    • Oh, D.K.1    Roh, H.J.2    Kim, S.Y.3    Noh, B.S.4
  • 7
    • 0347874223 scopus 로고    scopus 로고
    • Bioconversion of D-galactose to D-tagatose by expression of L-arabinose isomerase
    • Roh, H. J.; Kim, P.; Park, Y. C.; Choi, J. H. Bioconversion of D-galactose to D-tagatose by expression of L-arabinose isomerase. Biotechnol. Appl. Biochem. 2000, 31, 1-4.
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 1-4
    • Roh, H.J.1    Kim, P.2    Park, Y.C.3    Choi, J.H.4
  • 8
    • 0034048991 scopus 로고    scopus 로고
    • Preparation of L-arabinose isomerase originated from Escherichia coli as a bioatalyst for D-tagatose production
    • Roh, H. J.; Yoon, S. H.; Kim, P. Preparation of L-arabinose isomerase originated from Escherichia coli as a bioatalyst for D-tagatose production. Biotechnol. Lett. 2000, 22, 197-199.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 197-199
    • Roh, H.J.1    Yoon, S.H.2    Kim, P.3
  • 9
    • 0035121730 scopus 로고    scopus 로고
    • High production of D-tagatose, a potential sugar substitute, using immobilized L-arabinose isomerase
    • Kim, P.; Yoon, S. H.; Roh, H. J.; Choi, J. H. High production of D-tagatose, a potential sugar substitute, using immobilized L-arabinose isomerase. Biotechnol. Prog. 2001, 17, 208-210.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 208-210
    • Kim, P.1    Yoon, S.H.2    Roh, H.J.3    Choi, J.H.4
  • 10
    • 0035185226 scopus 로고    scopus 로고
    • Development of an immobilization method of L-arabinose isomerase for industrial production of tagatose
    • Oh, D. K.; Kim, H. J.; Ryu, S. A.; Kim, P. Development of an immobilization method of L-arabinose isomerase for industrial production of tagatose. Biotechnol. Lett. 2001, 23, 1859-1862.
    • (2001) Biotechnol. Lett. , vol.23 , pp. 1859-1862
    • Oh, D.K.1    Kim, H.J.2    Ryu, S.A.3    Kim, P.4
  • 11
    • 0037299866 scopus 로고    scopus 로고
    • Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production
    • Yoon, S. H.; Kim, P.; Oh, D. K. Properties of L-arabinose isomerase from Escherichia coli as biocatalyst for tagatose production. World J. Microbiol. Biotechnol. 2003, 19, 47-51.
    • (2003) World J. Microbiol. Biotechnol. , vol.19 , pp. 47-51
    • Yoon, S.H.1    Kim, P.2    Oh, D.K.3
  • 12
    • 0347254770 scopus 로고    scopus 로고
    • Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase
    • Kim, P.; Yoon, S. H.; Oh, D. K.; Choi, J. H. Improvement of tagatose conversion rate by genetic evolution of thermostable galactose isomerase. Biotechnol. Appl. Biochem. 2000, 31, 1-4.
    • (2000) Biotechnol. Appl. Biochem. , vol.31 , pp. 1-4
    • Kim, P.1    Yoon, S.H.2    Oh, D.K.3    Choi, J.H.4
  • 13
    • 0037357583 scopus 로고    scopus 로고
    • A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor
    • Kim, H. J.; Ryu, S. A.; Kim, P.; Oh, D. K. A feasible enzymatic process for D-tagatose production by an immobilized thermostable L-arabinose isomerase in a packed-bed bioreactor. Biotechnol. Prog. 2003, 19, 400-404.
    • (2003) Biotechnol. Prog. , vol.19 , pp. 400-404
    • Kim, H.J.1    Ryu, S.A.2    Kim, P.3    Oh, D.K.4
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugar and trioses
    • Dische, Z.; Borenfreund, E. A new spectrophotometric method for the detection and determination of keto sugar and trioses. J. Biol. Chem. 1951, 192, 583-587.
    • (1951) J. Biol. Chem. , vol.192 , pp. 583-587
    • Dische, Z.1    Borenfreund, E.2
  • 16
    • 0035899853 scopus 로고    scopus 로고
    • Computing radial packing properties from the distribution of particle centers
    • Mariani, N. J.; Martínez, O. M.; Barreto, G. F. Computing radial packing properties from the distribution of particle centers. Chem. Eng. Sci. 2001, 56, 5693-5707.
    • (2001) Chem. Eng. Sci. , vol.56 , pp. 5693-5707
    • Mariani, N.J.1    Martínez, O.M.2    Barreto, G.F.3
  • 17
    • 0034879083 scopus 로고    scopus 로고
    • Pressure-flow relationships for packed beds of compressible chromatography media at laboratory and production scale
    • Stickel, J. J.; Fotopoulos, A. Pressure-flow relationships for packed beds of compressible chromatography media at laboratory and production scale. Biotechnol. Prog. 2001, 17, 744-51.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 744-751
    • Stickel, J.J.1    Fotopoulos, A.2
  • 19
    • 0037139753 scopus 로고    scopus 로고
    • Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion
    • Petzelbauer, I.; Kuhn, B.; Splechtna, B.; Kulbe, K. D.; Nidetzky, B. Development of an ultrahigh-temperature process for the enzymatic hydrolysis of lactose. IV. Immobilization of two thermostable beta-glycosidases and optimization of a packed-bed reactor for lactose conversion. Biotechnol. Bioeng. 2002, 77, 619-31.
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 619-631
    • Petzelbauer, I.1    Kuhn, B.2    Splechtna, B.3    Kulbe, K.D.4    Nidetzky, B.5
  • 20
    • 0030767328 scopus 로고    scopus 로고
    • Production of high content inulo-oligosaccharides from inulinby a purified edoinulinase
    • Yun, J. H.; Kim, D. H.; Uhm, T. B.; Song, S. K. Production of high content inulo-oligosaccharides from inulinby a purified edoinulinase. Biotechnol. Lett. 1997, 19, 935-938.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 935-938
    • Yun, J.H.1    Kim, D.H.2    Uhm, T.B.3    Song, S.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.