메뉴 건너뛰기




Volumn 62, Issue 11, 2014, Pages 2412-2417

Coexpression of β-d-galactosidase and l-arabinose isomerase in the production of d-tagatose: A functional sweetener

Author keywords

coexpression; d tagatose; l arabinose isomerase; single step method; d galactosidase

Indexed keywords

GENES; INDUSTRIAL RESEARCH; SUGARS; ESCHERICHIA COLI; MANGANESE;

EID: 84896511457     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf4042485     Document Type: Article
Times cited : (36)

References (38)
  • 1
    • 0004670514 scopus 로고
    • Composition of the gum of Sterculia setigera: Occurrence of d -tagatose in nature
    • Hirst, E. L.; Hough, L.; Jones, J. K. N. Composition of the gum of Sterculia setigera: Occurrence of d -tagatose in nature Nature 1949, 163, 177
    • (1949) Nature , vol.163 , pp. 177
    • Hirst, E.L.1    Hough, L.2    Jones, J.K.N.3
  • 2
    • 0026728552 scopus 로고
    • Kinetics of galactose and tagatose formation during heat-treatment of milk
    • Troyono, E.; Martinez-Castro, I.; Olano, A. Kinetics of galactose and tagatose formation during heat-treatment of milk Food Chem. 1992, 45, 41-43
    • (1992) Food Chem. , vol.45 , pp. 41-43
    • Troyono, E.1    Martinez-Castro, I.2    Olano, A.3
  • 3
    • 0028839816 scopus 로고
    • Sugar substitutes: Their energy values, bulk characteristics, and potential health benefits
    • Levin, G. V.; Zehner, L. R.; Saunders, J. P.; Beadle, J. R. Sugar substitutes: Their energy values, bulk characteristics, and potential health benefits Am. J. Clin. Nutr. 1995, 62, 1161S-1168S
    • (1995) Am. J. Clin. Nutr. , vol.62
    • Levin, G.V.1    Zehner, L.R.2    Saunders, J.P.3    Beadle, J.R.4
  • 4
    • 17144375651 scopus 로고    scopus 로고
    • Chemical indicators of heat treatment in fortified and special milks
    • Mendoza, M. R.; Olano, A.; Villamiel, M. Chemical indicators of heat treatment in fortified and special milks J. Agric. Food Chem. 2005, 53, 2995-2999
    • (2005) J. Agric. Food Chem. , vol.53 , pp. 2995-2999
    • Mendoza, M.R.1    Olano, A.2    Villamiel, M.3
  • 5
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using l -arabinose isomerase, a review and future perspective
    • Kim, P. Current studies on biological tagatose production using l -arabinose isomerase, a review and future perspective Appl. Microbiol. Biotechnol. 2004, 65, 243-249
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 243-249
    • Kim, P.1
  • 6
    • 38049186809 scopus 로고    scopus 로고
    • Tagatose, a new antidiabetic and obesity control drug
    • Lu, Y.; Levin, G. V.; Donner, T. W. Tagatose, a new antidiabetic and obesity control drug Diabetes, Obes. Metab. 2008, 10, 109-134
    • (2008) Diabetes, Obes. Metab. , vol.10 , pp. 109-134
    • Lu, Y.1    Levin, G.V.2    Donner, T.W.3
  • 10
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: Properties, applications, and biotechnological processes
    • Oh, D. K. Tagatose: Properties, applications, and biotechnological processes Appl. Microbiol. Biotechnol. 2007, 76, 1-8
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 1-8
    • Oh, D.K.1
  • 11
    • 0027551680 scopus 로고
    • Bioconversion of d -galactose into d -tagatose
    • Cheetham, P. S. J.; Wootton, A. N. Bioconversion of d -galactose into d -tagatose Enzyme Microb. Technol. 1993, 15, 105-108
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 105-108
    • Cheetham, P.S.J.1    Wootton, A.N.2
  • 12
    • 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
  • 13
    • 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
  • 14
    • 36348972810 scopus 로고    scopus 로고
    • Characterization of an l -arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH
    • Chouayekh, H.; Bejar, W.; Rhimi, M.; Jelleli, K.; Mseddi, M.; Bejar, S. Characterization of an l -arabinose isomerase from the Lactobacillus plantarum NC8 strain showing pronounced stability at acidic pH FEMS Microbiol. Lett. 2007, 277, 260-267
    • (2007) FEMS Microbiol. Lett. , vol.277 , pp. 260-267
    • Chouayekh, H.1    Bejar, W.2    Rhimi, M.3    Jelleli, K.4    Mseddi, M.5    Bejar, S.6
  • 15
    • 79952814999 scopus 로고    scopus 로고
    • A novel l -arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d -tagatose production: Gene cloning, purification and characterization
    • Xu, Z.; Qing, Y.; Li, S.; Feng, X.; Xu, H.; Ouyang, P. A novel l -arabinose isomerase from Lactobacillus fermentum CGMCC2921 for d -tagatose production: Gene cloning, purification and characterization J. Mol. Catal. B: Enzym. 2011, 70, 1-7
    • (2011) J. Mol. Catal. B: Enzym. , vol.70 , pp. 1-7
    • Xu, Z.1    Qing, Y.2    Li, S.3    Feng, X.4    Xu, H.5    Ouyang, P.6
  • 16
    • 84865272522 scopus 로고    scopus 로고
    • A method for the production of d -tagatose using a recombinant Pichia pastoris strain secreting β- D -galactosidase from Arthrobacter chlorophenolicus and a recombinant l -arabinose isomerase from Arthrobacter sp. 22c
    • Wanarska, M.; Kur, J. A method for the production of d -tagatose using a recombinant Pichia pastoris strain secreting β- d -galactosidase from Arthrobacter chlorophenolicus and a recombinant l -arabinose isomerase from Arthrobacter sp. 22c Microb. Cell Fact. 2012, 11, 113
    • (2012) Microb. Cell Fact. , vol.11 , pp. 113
    • Wanarska, M.1    Kur, J.2
  • 17
    • 77955665578 scopus 로고    scopus 로고
    • The acid tolerant l -arabinose isomerase from the food grade Lactobacillus sakei 23 K is an attractive d -tagatose producer
    • Rhimi, M.; Ilhammami, R.; Bajic, G.; Boudebbouze, S.; Maguin, E.; Haser, R.; Aghajari, N. The acid tolerant l -arabinose isomerase from the food grade Lactobacillus sakei 23 K is an attractive d -tagatose producer Bioresour. Technol. 2010, 101, 9171-9177
    • (2010) Bioresour. Technol. , vol.101 , pp. 9171-9177
    • Rhimi, M.1    Ilhammami, R.2    Bajic, G.3    Boudebbouze, S.4    Maguin, E.5    Haser, R.6    Aghajari, N.7
  • 18
    • 84866740969 scopus 로고    scopus 로고
    • Bifidobacterium longum l -arabinose isomerase - Overexpression in Lactococcus lactis, purification, and characterization
    • Salonen, N.; Nyyssölä, A.; Salonen, K.; Turunen, O. Bifidobacterium longum l -arabinose isomerase-Overexpression in Lactococcus lactis, purification, and characterization Appl. Biochem. Biotechnol. 2012, 168, 392-405
    • (2012) Appl. Biochem. Biotechnol. , vol.168 , pp. 392-405
    • Salonen, N.1    Nyyssölä, A.2    Salonen, K.3    Turunen, O.4
  • 19
    • 0037742418 scopus 로고    scopus 로고
    • Production of tagatose by a recombinant thermostable l -arabinose isomerase from Thermus sp. IM6501
    • Kim, J. W.; Kim, Y. W.; Roh, H. J.; Kim, H. Y.; Cha, J. H.; Park, K. H.; Park, C. S. Production of tagatose by a recombinant thermostable l -arabinose isomerase from Thermus sp. IM6501 Biotechnol. Lett. 2003, 25, 963-967
    • (2003) Biotechnol. Lett. , vol.25 , pp. 963-967
    • Kim, J.W.1    Kim, Y.W.2    Roh, H.J.3    Kim, H.Y.4    Cha, J.H.5    Park, K.H.6    Park, C.S.7
  • 20
    • 34547920744 scopus 로고    scopus 로고
    • High production of d -tagatose by the addition of boric acid
    • Lim, B. C.; Kim, H. J.; Oh, D. K. High production of d -tagatose by the addition of boric acid Biotechnol. Prog. 2007, 23, 824-828
    • (2007) Biotechnol. Prog. , vol.23 , pp. 824-828
    • Lim, B.C.1    Kim, H.J.2    Oh, D.K.3
  • 21
    • 84880136941 scopus 로고    scopus 로고
    • D -Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum l -arabinose isomerase
    • Salonen, N.; Salonen, K.; Leisola, M.; Nyyssölä, A. d -Tagatose production in the presence of borate by resting Lactococcus lactis cells harboring Bifidobacterium longum l -arabinose isomerase Bioprocess Biosyst. Eng. 2013, 36, 489-497
    • (2013) Bioprocess Biosyst. Eng. , vol.36 , pp. 489-497
    • Salonen, N.1    Salonen, K.2    Leisola, M.3    Nyyssölä, A.4
  • 23
    • 84859004466 scopus 로고    scopus 로고
    • Lactose hydrolysis from milk/whey in batch and continuous processes by concanavalin A-Celite 545 immobilized Aspergillus oryzae β-galactosidase
    • Ansari, S. A.; Husain, Q. Lactose hydrolysis from milk/whey in batch and continuous processes by concanavalin A-Celite 545 immobilized Aspergillus oryzae β-galactosidase Food Bioprod. Process. 2012, 90, 351-359
    • (2012) Food Bioprod. Process. , vol.90 , pp. 351-359
    • Ansari, S.A.1    Husain, Q.2
  • 24
    • 0000767907 scopus 로고
    • The β- D -galactosidase of Escherichia coli srain K-12
    • Lederberg, J. The β- d -galactosidase of Escherichia coli srain K-12 J. Bacteriol. 1950, 60 (4) 381
    • (1950) J. Bacteriol. , vol.60 , Issue.4 , pp. 381
    • Lederberg, J.1
  • 25
    • 0001165802 scopus 로고
    • Purification, composition, and molecular weight of the β- D -galactosidase of Escherichia coli K12
    • Craven, G. R.; Steers, E.; Anfcnsen, C. B. Purification, composition, and molecular weight of the β- d -galactosidase of Escherichia coli K12 J. Biol. Chem. 1964, 240, 2468-2477
    • (1964) J. Biol. Chem. , vol.240 , pp. 2468-2477
    • Craven, G.R.1    Steers, E.2    Anfcnsen, C.B.3
  • 26
    • 0028178377 scopus 로고
    • Three-dimensional structure of β-galactosidase from E. Coli
    • Jacobson, R. H.; Zhang, X. J.; DuBose, R. F.; Matthews, B. W. Three-dimensional structure of β-galactosidase from E. coli Nature 1994, 369, 761-766
    • (1994) Nature , vol.369 , pp. 761-766
    • Jacobson, R.H.1    Zhang, X.J.2    Dubose, R.F.3    Matthews, B.W.4
  • 27
    • 84858749628 scopus 로고    scopus 로고
    • Production of d -tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells
    • Xu, Z.; Li, S.; Fu, F.; Li, G.; Feng, X.; Xu, H.; Ouyang, P. Production of d -tagatose, a functional sweetener, utilizing alginate immobilized Lactobacillus fermentum CGMCC2921 cells Appl. Biochem. Biotechnol. 2012, 166, 961-973
    • (2012) Appl. Biochem. Biotechnol. , vol.166 , pp. 961-973
    • Xu, Z.1    Li, S.2    Fu, F.3    Li, G.4    Feng, X.5    Xu, H.6    Ouyang, P.7
  • 28
    • 84899980900 scopus 로고    scopus 로고
    • Function of aspartic acid residues in optimum pH control l -arabinose isomerase from Lactobacillus fermentum
    • 10.1007/s00253-013-5342-7
    • Xu, Z.; Li, S.; Feng, X.; Zhan, Y.; Xu, H. Function of aspartic acid residues in optimum pH control l -arabinose isomerase from Lactobacillus fermentum Appl. Microbiol. Biotechnol. 2013, 10.1007/s00253-013-5342-7
    • (2013) Appl. Microbiol. Biotechnol.
    • Xu, Z.1    Li, S.2    Feng, X.3    Zhan, Y.4    Xu, H.5
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantitation 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
  • 30
    • 58349118740 scopus 로고    scopus 로고
    • Immobilization of β- D -galactosidase from Aspergillus oryzae via immunoaffinity support
    • Haider, T.; Husain, Q. Immobilization of β- d -galactosidase from Aspergillus oryzae via immunoaffinity support Biochem. Eng. J. 2009, 43, 307-314
    • (2009) Biochem. Eng. J. , vol.43 , pp. 307-314
    • Haider, T.1    Husain, Q.2
  • 31
    • 0346814641 scopus 로고
    • A new spectrophotometric method for the detection and determination of keto sugars and trioses
    • Dische, Z.; Borenfreund, E. A new spectrophotometric method for the detection and determination of keto sugars and trioses J. Biol. Chem. 1951, 192, 583-58
    • (1951) J. Biol. Chem. , vol.192 , pp. 583-658
    • Dische, Z.1    Borenfreund, E.2
  • 33
    • 26444526645 scopus 로고    scopus 로고
    • Purification and characterization of an l -arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d -tagatose
    • Kim, H. J.; Oh, D. K. Purification and characterization of an l -arabinose isomerase from an isolated strain of Geobacillus thermodenitrificans producing d -tagatose J. Biotechnol. 2005, 120, 162-173
    • (2005) J. Biotechnol. , vol.120 , pp. 162-173
    • Kim, H.J.1    Oh, D.K.2
  • 34
    • 77950629696 scopus 로고    scopus 로고
    • An l -arabinose isomerase from Acidothermus cellulolytics ATCC 43068: Cloning, expression, purification, and characterization
    • Cheng, L.; Mu, W.; Zhang, T.; Jiang, B. An l -arabinose isomerase from Acidothermus cellulolytics ATCC 43068: Cloning, expression, purification, and characterization Appl. Microbiol. Biotechnol. 2010, 86, 1089-1097
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 1089-1097
    • Cheng, L.1    Mu, W.2    Zhang, T.3    Jiang, B.4
  • 35
    • 33644629689 scopus 로고    scopus 로고
    • Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l -arabinose isomerase from the Bacillus stearothermophilus US100 strain
    • Rhimi, M.; Bejar, S. Cloning, purification and biochemical characterization of metallic-ions independent and thermoactive l -arabinose isomerase from the Bacillus stearothermophilus US100 strain Biochim. Biophys. Acta 2006, 1760, 191-199
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 191-199
    • Rhimi, M.1    Bejar, S.2
  • 36
    • 0037129833 scopus 로고    scopus 로고
    • Cloning, expression and characterization of l -arabinose isomerase from Thermotoga neapolitana: Bioconversion of d -galactose to d -tagatose using the enzyme
    • Kim, B. C.; Lee, Y. H.; Lee, H. S.; Lee, D. W.; Choe, E. A.; Pyun, Y. R. Cloning, expression and characterization of l -arabinose isomerase from Thermotoga neapolitana: Bioconversion of d -galactose to d -tagatose using the enzyme FEMS Microbiol. Lett. 2002, 212, 121-126
    • (2002) FEMS Microbiol. Lett. , vol.212 , pp. 121-126
    • Kim, B.C.1    Lee, Y.H.2    Lee, H.S.3    Lee, D.W.4    Choe, E.A.5    Pyun, Y.R.6
  • 37
    • 1642416740 scopus 로고    scopus 로고
    • Characterization of a thermostable l -arabinose (d -galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima
    • Lee, D. W.; Jang, H. J.; Choe, E. A.; Kim, B. C.; Lee, S. J.; Kim, S. B.; Hong, Y. H.; Pyun, Y. R. Characterization of a thermostable l -arabinose (d -galactose) isomerase from the hyperthermophilic eubacterium Thermotoga maritima Appl. Environ. Microbiol. 2004, 70, 1397-1404
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1397-1404
    • Lee, D.W.1    Jang, H.J.2    Choe, E.A.3    Kim, B.C.4    Lee, S.J.5    Kim, S.B.6    Hong, Y.H.7    Pyun, Y.R.8
  • 38
    • 79955525190 scopus 로고    scopus 로고
    • Identification and characterization of a novel l -arabinose isomerase from Anoxybacillus flavithermus useful in d -tagatose production
    • Li, Y.; Zhu, Y.; Liu, A.; Sun, Y. Identification and characterization of a novel l -arabinose isomerase from Anoxybacillus flavithermus useful in d -tagatose production Extremophiles 2011, 15, 441-450
    • (2011) Extremophiles , vol.15 , pp. 441-450
    • Li, Y.1    Zhu, Y.2    Liu, A.3    Sun, Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.