메뉴 건너뛰기




Volumn 49, Issue 12, 2014, Pages 2134-2140

Evaluation of the cold-active Pseudoalteromonas haloplanktis β-galactosidase enzyme for lactose hydrolysis in whey permeate as primary step of d-tagatose production

Author keywords

Cold active galactosidase; Enzymatic hydrolysis; Lactose; Pseudoalteromonas haloplanktis; Whey permeate

Indexed keywords

BEVERAGES; GLUCOSE; HYDROLYSIS; SUGARS;

EID: 84936999103     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2014.09.010     Document Type: Article
Times cited : (40)

References (40)
  • 1
    • 0030199270 scopus 로고    scopus 로고
    • The biotechnological utilization of cheese whey: A review
    • M.I. Gonzalez Siso The biotechnological utilization of cheese whey: a review Bioresour Technol 57 1996 1 11
    • (1996) Bioresour Technol , vol.57 , pp. 1-11
    • Gonzalez Siso, M.I.1
  • 2
  • 3
    • 0035319361 scopus 로고    scopus 로고
    • Cold-adapted β-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis
    • A. Hoyoux, I. Jennes, P. Dubois, S. Genicot, F. Dubail, and J.M. François Cold-adapted β-galactosidase from the Antarctic psychrophile Pseudoalteromonas haloplanktis Appl Environ Microb 67 4 2001 1529 1535
    • (2001) Appl Environ Microb , vol.67 , Issue.4 , pp. 1529-1535
    • Hoyoux, A.1    Jennes, I.2    Dubois, P.3    Genicot, S.4    Dubail, F.5    François, J.M.6
  • 5
    • 84867033181 scopus 로고    scopus 로고
    • Optimization and modeling of lactose hydrolysis in a packed bed system using immobilized β-galactosidase from Aspergillus oryzae
    • J. Fischer, C.Z. Guidini, L.N. Soares Santana, M.M. de Resende, V.L. Cardoso, and E.J. Ribeiro Optimization and modeling of lactose hydrolysis in a packed bed system using immobilized β-galactosidase from Aspergillus oryzae J Mol Catal B: Enzym 85-86 2013 178 186
    • (2013) J Mol Catal B: Enzym , vol.85-86 , pp. 178-186
    • Fischer, J.1    Guidini, C.Z.2    Soares Santana, L.N.3    De Resende, M.M.4    Cardoso, V.L.5    Ribeiro, E.J.6
  • 6
    • 0002432061 scopus 로고    scopus 로고
    • Production of β-galactosidase for lactose hydrolysis in milk and dairy products using thermophilic lactic acid bacteria
    • T. Vasiljevic, and P. Jelen Production of β-galactosidase for lactose hydrolysis in milk and dairy products using thermophilic lactic acid bacteria Innov Food Sci Technol 2 2001 75 85
    • (2001) Innov Food Sci Technol , vol.2 , pp. 75-85
    • Vasiljevic, T.1    Jelen, P.2
  • 7
    • 58349094180 scopus 로고    scopus 로고
    • Hydrolysis of milk/whey lactose by β-galactosidase: A comparative study of stirred batch process and packed bed reactor prepared with calcium alginate entrapped enzyme
    • T. Haider, and Q. Husain Hydrolysis of milk/whey lactose by β-galactosidase: a comparative study of stirred batch process and packed bed reactor prepared with calcium alginate entrapped enzyme Chem Eng Process 48 2009 576 580
    • (2009) Chem Eng Process , vol.48 , pp. 576-580
    • Haider, T.1    Husain, Q.2
  • 8
    • 0344153356 scopus 로고    scopus 로고
    • Lactose hydrolysis by Lactozym™ immobilized on cellulose beads in batch and fluidized bed modes
    • I. Roy, and M.N. Gupta Lactose hydrolysis by Lactozym™ immobilized on cellulose beads in batch and fluidized bed modes Process Biochem 39 2003 325 332
    • (2003) Process Biochem , vol.39 , pp. 325-332
    • Roy, I.1    Gupta, M.N.2
  • 9
    • 0034748951 scopus 로고    scopus 로고
    • Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis
    • Q.Z.K. Zhou, and X. Dong Chen Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis Biochem Eng J 9 2001 33 40
    • (2001) Biochem Eng J , vol.9 , pp. 33-40
    • Zhou, Q.Z.K.1    Dong Chen, X.2
  • 10
    • 0033527096 scopus 로고    scopus 로고
    • Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-glycosidases
    • I. Petzelbauer, B. Nidetzky, D. Haltrich, and K.D. Kulbe Development of an ultra-high-temperature process for the enzymatic hydrolysis of lactose. I. The properties of two thermostable β-glycosidases Biotechnol Bioeng 64 3 1999 322 332
    • (1999) Biotechnol Bioeng , vol.64 , Issue.3 , pp. 322-332
    • Petzelbauer, I.1    Nidetzky, B.2    Haltrich, D.3    Kulbe, K.D.4
  • 11
    • 0037454636 scopus 로고    scopus 로고
    • Hydrolysis of lactose by free and immobilized β-galactosidase from Thermus sp. Strain T2
    • M. Ladero, M.T. Perez, and F. Garcia-Ochoa Hydrolysis of lactose by free and immobilized β-galactosidase from Thermus sp. strain T2 Biotechnol Bioeng 81 2 2003 241 252
    • (2003) Biotechnol Bioeng , vol.81 , Issue.2 , pp. 241-252
    • Ladero, M.1    Perez, M.T.2    Garcia-Ochoa, F.3
  • 13
    • 4544346270 scopus 로고    scopus 로고
    • Current studies on biological tagatose production using l-arabinose isomerase: A review and future perspective
    • P. Kim Current studies on biological tagatose production using l-arabinose isomerase: a review and future perspective Appl Microbiol Biot 65 2004 243 249
    • (2004) Appl Microbiol Biot , vol.65 , pp. 243-249
    • Kim, P.1
  • 16
    • 34547600568 scopus 로고    scopus 로고
    • Tagatose: Properties, applications and biotechnological processes
    • D.-K. Oh Tagatose: properties, applications and biotechnological processes Appl Microbiol Biot 76 2007 1 8
    • (2007) Appl Microbiol Biot , vol.76 , pp. 1-8
    • Oh, D.-K.1
  • 17
    • 38049186809 scopus 로고    scopus 로고
    • Tagatose, a new antidiabetic and obesity control drug
    • Y. Lu, G.V. Levin, and T.W. Donner Tagatose, a new antidiabetic and obesity control drug Diab Obes Metab 10 2008 109 134
    • (2008) Diab Obes Metab , vol.10 , pp. 109-134
    • Lu, Y.1    Levin, G.V.2    Donner, T.W.3
  • 21
    • 0034333646 scopus 로고    scopus 로고
    • Hydrolysis of lactose in whey permeate by immobilized β-galactosidase from Kluyveromyces fragilis
    • J. Szczodrak Hydrolysis of lactose in whey permeate by immobilized β-galactosidase from Kluyveromyces fragilis J Mol Catal B: Enzym 10 2000 631 637
    • (2000) J Mol Catal B: Enzym , vol.10 , pp. 631-637
    • Szczodrak, J.1
  • 22
    • 3142713057 scopus 로고    scopus 로고
    • Enzymatic conversion of d-galactose to d-tagatose: Heterologous expression and characterisation of a thermostable l-arabinose isomerase from Thermoanaerobacter mathranii
    • F. Jørgensen, O.C. Hansen, and P. Stougaard Enzymatic conversion of d-galactose to d-tagatose: heterologous expression and characterisation of a thermostable l-arabinose isomerase from Thermoanaerobacter mathranii Appl Microbiol Biot 64 2004 816 822
    • (2004) Appl Microbiol Biot , vol.64 , pp. 816-822
    • Jørgensen, F.1    Hansen, O.C.2    Stougaard, P.3
  • 23
    • 64449084435 scopus 로고    scopus 로고
    • Rational design of Bacillus stearothermophilus US100 l-arabinose isomerase: Potential applications for d-tagatose production
    • M. Rhimi, N. Aghajari, M. Juy, H. Chouayekh, E. Maguin, and R. Haser Rational design of Bacillus stearothermophilus US100 l-arabinose isomerase: potential applications for d-tagatose production Biochimie 91 2009 650 653
    • (2009) Biochimie , vol.91 , pp. 650-653
    • Rhimi, M.1    Aghajari, N.2    Juy, M.3    Chouayekh, H.4    Maguin, E.5    Haser, R.6
  • 24
    • 11444258321 scopus 로고    scopus 로고
    • Distinct metal dependence for catalytic and structural functions in the l-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus
    • D.-W. Lee, E.-A. Choe, S.-B. Kim, S.-H. Eom, Y.-H. Hong, and S.-J. Lee Distinct metal dependence for catalytic and structural functions in the l-arabinose isomerases from the mesophilic Bacillus halodurans and the thermophilic Geobacillus stearothermophilus Arch Biochem Biophys 434 2005 333 343
    • (2005) Arch Biochem Biophys , vol.434 , pp. 333-343
    • Lee, D.-W.1    Choe, E.-A.2    Kim, S.-B.3    Eom, S.-H.4    Hong, Y.-H.5    Lee, S.-J.6
  • 25
    • 0002976888 scopus 로고
    • Hydrolysis of lactose: A literature review
    • V. Gekas, and M. Lopez-Leiva Hydrolysis of lactose: a literature review Process Biochem 20 1985 2 12
    • (1985) Process Biochem , vol.20 , pp. 2-12
    • Gekas, V.1    Lopez-Leiva, M.2
  • 26
    • 76649107887 scopus 로고    scopus 로고
    • Galacto-oligosaccharide production using microbial β-galactosidase: Current state and perspectives
    • A.R. Park, and D.K. Oh Galacto-oligosaccharide production using microbial β-galactosidase: current state and perspectives Appl Microbiol Biot 85 2010 1279 1286
    • (2010) Appl Microbiol Biot , vol.85 , pp. 1279-1286
    • Park, A.R.1    Oh, D.K.2
  • 27
    • 79959999611 scopus 로고    scopus 로고
    • Potential applications of immobilized β-galactosidase in food processing industries
    • 16 pp. Article ID 473137
    • P.S. Panesar, S. Kumari, and R. Panesar Potential applications of immobilized β-galactosidase in food processing industries Enzyme Res 2010 2010 16 pp. Article ID 473137
    • (2010) Enzyme Res , vol.2010
    • Panesar, P.S.1    Kumari, S.2    Panesar, R.3
  • 28
    • 83455189631 scopus 로고    scopus 로고
    • Enzymes in food processing: A condensed overview on strategies for better biocatalysts
    • 19 pp. Article ID 862537
    • P. Fernandes Enzymes in food processing: a condensed overview on strategies for better biocatalysts Enzyme Res 2010 2010 19 pp. Article ID 862537
    • (2010) Enzyme Res , vol.2010
    • Fernandes, P.1
  • 30
    • 70350200860 scopus 로고    scopus 로고
    • A new β-galactosidase with a low temperature optimum isolated from the Antarctic Arthrobacter sp. 20B: Gene cloning, expression and characterization
    • A.M. Bialkowska, H. Cieslinski, K.M. Nowakowska, J. Kur, and M. Turkiewicz A new β-galactosidase with a low temperature optimum isolated from the Antarctic Arthrobacter sp. 20B: gene cloning, expression and characterization Arch Microbiol 191 2009 825 835
    • (2009) Arch Microbiol , vol.191 , pp. 825-835
    • Bialkowska, A.M.1    Cieslinski, H.2    Nowakowska, K.M.3    Kur, J.4    Turkiewicz, M.5
  • 31
    • 28844447818 scopus 로고    scopus 로고
    • Cold-active acid β-galactosidase activity of isolated psychrophilic-basidiomycetous yeast Guehomyces pullulans
    • T. Nakagawa, R. Ikehata, M. Uchino, T. Miyaji, K. Takano, and N. Tomizuka Cold-active acid β-galactosidase activity of isolated psychrophilic-basidiomycetous yeast Guehomyces pullulans Microbiol Res 161 2006 75 79
    • (2006) Microbiol Res , vol.161 , pp. 75-79
    • Nakagawa, T.1    Ikehata, R.2    Uchino, M.3    Miyaji, T.4    Takano, K.5    Tomizuka, N.6
  • 32
    • 34249074067 scopus 로고    scopus 로고
    • Overexpression and functional analysis of cold-active β-galactosidase from Arthrobacter psychrolactophilus strain F2
    • T. Nakagawa, R. Ikehata, T. Myoda, T. Miyaji, and N. Tomizuka Overexpression and functional analysis of cold-active β-galactosidase from Arthrobacter psychrolactophilus strain F2 Protein Expr Purif 54 2007 295 299
    • (2007) Protein Expr Purif , vol.54 , pp. 295-299
    • Nakagawa, T.1    Ikehata, R.2    Myoda, T.3    Miyaji, T.4    Tomizuka, N.5
  • 33
    • 33846248256 scopus 로고    scopus 로고
    • Immobilized preparation of cold-adapted and halotolerant Antarctic β-galactosidase as a highly stable catalyst in lactose hydrolysis
    • K. Makowski, A. Bialkowska, H. Szczęsna-Antczak Kalinowska, J. Kur, H. Cieslinski, and M. Turkiewicz Immobilized preparation of cold-adapted and halotolerant Antarctic β-galactosidase as a highly stable catalyst in lactose hydrolysis FEMS Microbiol Ecol 59 2007 535 542
    • (2007) FEMS Microbiol Ecol , vol.59 , pp. 535-542
    • Makowski, K.1    Bialkowska, A.2    Szczęsna-Antczak Kalinowska, H.3    Kur, J.4    Cieslinski, H.5    Turkiewicz, M.6
  • 34
    • 0033946342 scopus 로고    scopus 로고
    • A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures
    • D. Georlette, Z.O. Jonsson, F. Van Petegem, J.P. Chessa, J. Van Beeumen, and U. Hübscher A DNA ligase from the psychrophile Pseudoalteromonas haloplanktis gives insights into the adaptation of proteins to low temperatures Eur J Biochem 267 2000 3502 3512
    • (2000) Eur J Biochem , vol.267 , pp. 3502-3512
    • Georlette, D.1    Jonsson, Z.O.2    Van Petegem, F.3    Chessa, J.P.4    Van Beeumen, J.5    Hübscher, U.6
  • 35
    • 0037688133 scopus 로고    scopus 로고
    • Molecular adaptations to cold in psychrophilic enzymes. Review
    • G. Feller Molecular adaptations to cold in psychrophilic enzymes. Review Cell Mol Life Sci 60 2003 648 662
    • (2003) Cell Mol Life Sci , vol.60 , pp. 648-662
    • Feller, G.1
  • 36
    • 25844462537 scopus 로고    scopus 로고
    • Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TACl25
    • C. Médigue, E. Krin, G. Pascal, V. Barbe, A. Bernsel, and P.N. Bertin Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TACl25 Genome Res 15 2005 1325 1335
    • (2005) Genome Res , vol.15 , pp. 1325-1335
    • Médigue, C.1    Krin, E.2    Pascal, G.3    Barbe, V.4    Bernsel, A.5    Bertin, P.N.6
  • 37
    • 70349411614 scopus 로고    scopus 로고
    • Evolved β-galactosidases from Geobacillus stearothermophilus with improved transgalactosylation yield for galacto-oligosaccharide production
    • G. Placier, H. Watzlawick, C. Rabiller, and R. Mattes Evolved β-galactosidases from Geobacillus stearothermophilus with improved transgalactosylation yield for galacto-oligosaccharide production Appl Environ Microb 75 19 2009 6312 6321
    • (2009) Appl Environ Microb , vol.75 , Issue.19 , pp. 6312-6321
    • Placier, G.1    Watzlawick, H.2    Rabiller, C.3    Mattes, R.4
  • 38
    • 0000825201 scopus 로고
    • Oligosaccharide structures formed during the hydrolysis of lactose by Aspergillus oryzae β-galactosidase
    • T. Toba, A. Yokota, and S. Adachi Oligosaccharide structures formed during the hydrolysis of lactose by Aspergillus oryzae β-galactosidase Food Chem 16 1985 147 162
    • (1985) Food Chem , vol.16 , pp. 147-162
    • Toba, T.1    Yokota, A.2    Adachi, S.3
  • 39
    • 0025917587 scopus 로고
    • Oligosaccharide structures formed during acid hydrolysis of lactose
    • K.T. Huh, T. Toba, and S. Adachi Oligosaccharide structures formed during acid hydrolysis of lactose Food Chem 39 1991 39 49
    • (1991) Food Chem , vol.39 , pp. 39-49
    • Huh, K.T.1    Toba, T.2    Adachi, S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.