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Volumn 81, Issue , 2013, Pages 54-64

Hydrolysis of lactose in whole milk catalyzed by β-galactosidase from Kluyveromyces fragilis immobilized on chitosan-based matrix

Author keywords

Galactosidase; Batch processing; Chitosan; Immobilized enzymes; Lactose; Whole milk

Indexed keywords

DIFFERENT PROTOCOLS; GALACTOSIDASES; IMMOBILIZED BIOCATALYSTS; IMMOBILIZED ENZYME; INITIAL ACTIVITY; KLUYVEROMYCES FRAGILIS; LACTOSE; WHOLE MILK;

EID: 84887004978     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2013.10.007     Document Type: Article
Times cited : (38)

References (50)
  • 2
    • 84886997234 scopus 로고    scopus 로고
    • Experimental study of lactose hydrolysis and separation in continuous stirred tank-ultrafiltration membrane reactor
    • Pakizeh M., Namvar-Mahboub M. Experimental study of lactose hydrolysis and separation in continuous stirred tank-ultrafiltration membrane reactor. J. Chem. Eng. Process 2011, 2:1-4.
    • (2011) J. Chem. Eng. Process , vol.2 , pp. 1-4
    • Pakizeh, M.1    Namvar-Mahboub, M.2
  • 3
    • 83055176319 scopus 로고    scopus 로고
    • Lactose hydrolysis and other conversions in dairy products: technological aspects
    • Harju M., Kallioinen H., Tossavainen O. Lactose hydrolysis and other conversions in dairy products: technological aspects. Int. Dairy J. 2012, 22:104-109.
    • (2012) Int. Dairy J. , vol.22 , pp. 104-109
    • Harju, M.1    Kallioinen, H.2    Tossavainen, O.3
  • 4
    • 0032524182 scopus 로고    scopus 로고
    • Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromyces fragilis
    • Santos A., Ladero M., García-Ochoa F. Kinetic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromyces fragilis. Enzyme Microb. Technol. 1998, 22:558-567.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 558-567
    • Santos, A.1    Ladero, M.2    García-Ochoa, F.3
  • 5
    • 18144421570 scopus 로고    scopus 로고
    • Modeling of the simultaneous hydrolysis-ultratfiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger
    • Hatzinikolaou G.D., Katsifas E., Mamma D., Karagouni D.A., Christakopoulos P., Kekos D. Modeling of the simultaneous hydrolysis-ultratfiltration of whey permeate by a thermostable β-galactosidase from Aspergillus niger. Biochem. Eng. J. 2005, 24:161-172.
    • (2005) Biochem. Eng. J. , vol.24 , pp. 161-172
    • Hatzinikolaou, G.D.1    Katsifas, E.2    Mamma, D.3    Karagouni, D.A.4    Christakopoulos, P.5    Kekos, D.6
  • 6
    • 24044488301 scopus 로고    scopus 로고
    • A new innovate process to produce lactose-reduced skim milk
    • Novalin S., Neuhaus W., Kulbe D.K. A new innovate process to produce lactose-reduced skim milk. J. Biotechnol. 2005, 119:212-218.
    • (2005) J. Biotechnol. , vol.119 , pp. 212-218
    • Novalin, S.1    Neuhaus, W.2    Kulbe, D.K.3
  • 8
    • 0034333338 scopus 로고    scopus 로고
    • Kinetic modeling of lactose hydrolysis with an immobilized β-galactosidase from Kluyveromyces fragilis
    • Ladero M., Santos A., Garcia-Ochoa F. Kinetic modeling of lactose hydrolysis with an immobilized β-galactosidase from Kluyveromyces fragilis. Enzyme Microb. Technol. 2000, 27:583-592.
    • (2000) Enzyme Microb. Technol. , vol.27 , pp. 583-592
    • Ladero, M.1    Santos, A.2    Garcia-Ochoa, F.3
  • 9
    • 0002976888 scopus 로고
    • Hydrolysis of lactose: a literature review
    • Gekas V., Lopez-Leiva M.L. Hydrolysis of lactose: a literature review. Process Biochem. 1985, 20:2-12.
    • (1985) Process Biochem. , vol.20 , pp. 2-12
    • Gekas, V.1    Lopez-Leiva, M.L.2
  • 10
    • 84986435959 scopus 로고
    • Stability and enzymatic propetiers of β-galactosidase from Kluyveromyces fragilis
    • Mahoney R.R., Whitaker R.J. Stability and enzymatic propetiers of β-galactosidase from Kluyveromyces fragilis. J. Food Biochem. 1977, 1:327-350.
    • (1977) J. Food Biochem. , vol.1 , pp. 327-350
    • Mahoney, R.R.1    Whitaker, R.J.2
  • 14
    • 52649166805 scopus 로고    scopus 로고
    • Improving the properties of chitosan as support for the covalent multipoint immobilization of chymotrypsin
    • Adriano W.S., Mendonça D.B., Rodrigues D.S., Mammarella E.J., Giordano R.L.C. Improving the properties of chitosan as support for the covalent multipoint immobilization of chymotrypsin. Biomacromolecules 2008, 9:2170-2179.
    • (2008) Biomacromolecules , vol.9 , pp. 2170-2179
    • Adriano, W.S.1    Mendonça, D.B.2    Rodrigues, D.S.3    Mammarella, E.J.4    Giordano, R.L.C.5
  • 15
    • 80051704822 scopus 로고    scopus 로고
    • Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts
    • Mendes A.A., Castro H.F., Rodrigues D.S., Adriano W.S., Tardioli P.W., Mammarella E.J., Giordano R.C., Giordano R.L.C. Multipoint covalent immobilization of lipase on chitosan hybrid hydrogels: influence of the polyelectrolyte complex type and chemical modification on the catalytic properties of the biocatalysts. J. Ind. Microbiol. Biotechnol. 2011, 38:1055-1066.
    • (2011) J. Ind. Microbiol. Biotechnol. , vol.38 , pp. 1055-1066
    • Mendes, A.A.1    Castro, H.F.2    Rodrigues, D.S.3    Adriano, W.S.4    Tardioli, P.W.5    Mammarella, E.J.6    Giordano, R.C.7    Giordano, R.L.C.8
  • 16
    • 38049011348 scopus 로고    scopus 로고
    • Stabilization of quaternary structure of a hexameric alpha-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques
    • Pessela B.C., Mateo C., Filho M., Carrascosa A.V., Fernández-Lafuente R., Guisán J.M. Stabilization of quaternary structure of a hexameric alpha-galactosidase from Thermus sp. T2 by immobilization and post-immobilization techniques. Process Biochem. 2008, 43:193-198.
    • (2008) Process Biochem. , vol.43 , pp. 193-198
    • Pessela, B.C.1    Mateo, C.2    Filho, M.3    Carrascosa, A.V.4    Fernández-Lafuente, R.5    Guisán, J.M.6
  • 17
    • 58149296120 scopus 로고    scopus 로고
    • The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits. Stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports
    • Bolivar J.M., Mateo C., Rocha-Martin J., Cava F., Berenguer J., Fernandez-Lafuente R., Guisan J.M. The adsorption of multimeric enzymes on very lowly activated supports involves more enzyme subunits. Stabilization of a glutamate dehydrogenase from Thermus thermophilus by immobilization on heterofunctional supports. Enzyme Microb. Technol. 2009, 44:139-144.
    • (2009) Enzyme Microb. Technol. , vol.44 , pp. 139-144
    • Bolivar, J.M.1    Mateo, C.2    Rocha-Martin, J.3    Cava, F.4    Berenguer, J.5    Fernandez-Lafuente, R.6    Guisan, J.M.7
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins 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
  • 19
    • 84887013702 scopus 로고    scopus 로고
    • Estudio del proceso conjunto de recuperación de proteínas e hidrólisis de lactosa presentes en el suero dulce de quesería en una unidad de ultrafiltración con enzimas immovilizadas
    • Torres A.A., Regenhardt A.S., Mammarela E.J., Rubiolo A.C. Estudio del proceso conjunto de recuperación de proteínas e hidrólisis de lactosa presentes en el suero dulce de quesería en una unidad de ultrafiltración con enzimas immovilizadas. Interamerican Confederation of Chemical Engeneering (CIIQ) 2006.
    • (2006) Interamerican Confederation of Chemical Engeneering (CIIQ)
    • Torres, A.A.1    Regenhardt, A.S.2    Mammarela, E.J.3    Rubiolo, A.C.4
  • 20
    • 0003072603 scopus 로고
    • Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor
    • Trinder P. Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor. Ann. Clin. Biochem. 1969, 6:24-27.
    • (1969) Ann. Clin. Biochem. , vol.6 , pp. 24-27
    • Trinder, P.1
  • 23
    • 33747050939 scopus 로고    scopus 로고
    • Chitosan gel formation via the chitosan-epichlorohydrin adduct and its subsequent mineralization with hydroxyapatite
    • Fangkangwanwong J., Yoksan R., Chirachanchai S. Chitosan gel formation via the chitosan-epichlorohydrin adduct and its subsequent mineralization with hydroxyapatite. Polymer 2006, 47:6438-6445.
    • (2006) Polymer , vol.47 , pp. 6438-6445
    • Fangkangwanwong, J.1    Yoksan, R.2    Chirachanchai, S.3
  • 24
    • 0024029957 scopus 로고
    • Aldehyde gels as activated support for immobilization-stabilization of enzymes
    • Guisán J.M. Aldehyde gels as activated support for immobilization-stabilization of enzymes. Enzyme Microb. Technol. 1988, 10:375-382.
    • (1988) Enzyme Microb. Technol. , vol.10 , pp. 375-382
    • Guisán, J.M.1
  • 25
  • 27
    • 0023435073 scopus 로고
    • Single-step unimolecular non-first-order enzyme deactivation kinetics
    • Sadana A., Henley J.P. Single-step unimolecular non-first-order enzyme deactivation kinetics. Biotechnol. Bioeng. 1987, 30:717-723.
    • (1987) Biotechnol. Bioeng. , vol.30 , pp. 717-723
    • Sadana, A.1    Henley, J.P.2
  • 29
    • 0037070488 scopus 로고    scopus 로고
    • Studies on the activity and the stability of β-galactosidases from Thermus sp. strain T2 and from Kluyveromyces fragilis
    • Ladero M., Santos A., Garcia L.J., Carrascosa A.V., Pessela B.C.C., Garcia-Ochoa F. Studies on the activity and the stability of β-galactosidases from Thermus sp. strain T2 and from Kluyveromyces fragilis. Enzyme Microb. Technol. 2002, 30:392-405.
    • (2002) Enzyme Microb. Technol. , vol.30 , pp. 392-405
    • Ladero, M.1    Santos, A.2    Garcia, L.J.3    Carrascosa, A.V.4    Pessela, B.C.C.5    Garcia-Ochoa, F.6
  • 30
    • 70349782241 scopus 로고    scopus 로고
    • Stabilization of multimeric enzymes: strategies to prevent subunit dissociation
    • Fernandez-Lafuente R. Stabilization of multimeric enzymes: strategies to prevent subunit dissociation. Enzyme Microb. Technol. 2009, 45:405-418.
    • (2009) Enzyme Microb. Technol. , vol.45 , pp. 405-418
    • Fernandez-Lafuente, R.1
  • 31
    • 77956170052 scopus 로고    scopus 로고
    • Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: amino-glyoxyl versus amino-epoxy supports
    • Bolivar J.M., Mateo C., Grazu V., Carrascosa A.V., Pessela B.C., Guisan J.M. Heterofunctional supports for the one-step purification, immobilization and stabilization of large multimeric enzymes: amino-glyoxyl versus amino-epoxy supports. Process Biochem. 2010, 45:1692-1698.
    • (2010) Process Biochem. , vol.45 , pp. 1692-1698
    • Bolivar, J.M.1    Mateo, C.2    Grazu, V.3    Carrascosa, A.V.4    Pessela, B.C.5    Guisan, J.M.6
  • 33
    • 3142763845 scopus 로고    scopus 로고
    • Application of chitin- and chitosan-based materials for enzyme immobilizations: a review
    • Krajewska B. Application of chitin- and chitosan-based materials for enzyme immobilizations: a review. Enzyme Microb. Technol. 2004, 35:126-139.
    • (2004) Enzyme Microb. Technol. , vol.35 , pp. 126-139
    • Krajewska, B.1
  • 34
    • 0346094228 scopus 로고    scopus 로고
    • Structure and interactions in covalently and ionically crosslinked chitosan hydrogels for biomedical applications
    • Berger J., Reist M., Mayer J.M., Felt O., Peppas N.A., Gurny R. Structure and interactions in covalently and ionically crosslinked chitosan hydrogels for biomedical applications. Eur. J. Pharm. Biopharm. 2004, 57:19-34.
    • (2004) Eur. J. Pharm. Biopharm. , vol.57 , pp. 19-34
    • Berger, J.1    Reist, M.2    Mayer, J.M.3    Felt, O.4    Peppas, N.A.5    Gurny, R.6
  • 35
    • 0346724867 scopus 로고    scopus 로고
    • Comparative studies on polyelectrolyte complexes and mixtures of chitosan-alginate and chitosan-carrageenan as prolonged diltiazem clorhydrate release systems
    • Tapia C., Escobar Z., Costa E., Sapag-Hagar J., Valenzuela F., Basualto C., Gai M.N., Yazdani-Pedram M. Comparative studies on polyelectrolyte complexes and mixtures of chitosan-alginate and chitosan-carrageenan as prolonged diltiazem clorhydrate release systems. Eur. J. Pharm. Biopharm. 2004, 57:65-75.
    • (2004) Eur. J. Pharm. Biopharm. , vol.57 , pp. 65-75
    • Tapia, C.1    Escobar, Z.2    Costa, E.3    Sapag-Hagar, J.4    Valenzuela, F.5    Basualto, C.6    Gai, M.N.7    Yazdani-Pedram, M.8
  • 36
    • 0030294928 scopus 로고    scopus 로고
    • Calcium-alginate beads coated with chitosan: effect of the structure of encapsulated materials on their release
    • Huguet M.L., Dellacherie E. Calcium-alginate beads coated with chitosan: effect of the structure of encapsulated materials on their release. Process Biochem. 1996, 31:745-751.
    • (1996) Process Biochem. , vol.31 , pp. 745-751
    • Huguet, M.L.1    Dellacherie, E.2
  • 37
    • 33746474818 scopus 로고    scopus 로고
    • Polyionic hydrocolloids for the intestinal delivery of protein drugs: alginate and chitosan-a review
    • George M., Abraham T.E. Polyionic hydrocolloids for the intestinal delivery of protein drugs: alginate and chitosan-a review. J. Control. Release 2006, 114:1-14.
    • (2006) J. Control. Release , vol.114 , pp. 1-14
    • George, M.1    Abraham, T.E.2
  • 38
    • 0347995141 scopus 로고    scopus 로고
    • Application of chitosan-entrapped β-galactosidase in a packed-bed reactor system
    • Wentworth D.S., Skonberg D., Donahue D.W., Ghanem A. Application of chitosan-entrapped β-galactosidase in a packed-bed reactor system. J. Appl. Polym. Sci. 2004, 91:1294-1299.
    • (2004) J. Appl. Polym. Sci. , vol.91 , pp. 1294-1299
    • Wentworth, D.S.1    Skonberg, D.2    Donahue, D.W.3    Ghanem, A.4
  • 39
    • 84870196531 scopus 로고    scopus 로고
    • Preparation and application of epoxy-chitosan/alginate support in the immobilization of microbial lipases by covalent attachment
    • Mendes A.A., Castro H.F., Andrade G.S.S., Tardioli P.W., Giordano R.L.C. Preparation and application of epoxy-chitosan/alginate support in the immobilization of microbial lipases by covalent attachment. React. Funct. Polym. 2013, 73:160-167.
    • (2013) React. Funct. Polym. , vol.73 , pp. 160-167
    • Mendes, A.A.1    Castro, H.F.2    Andrade, G.S.S.3    Tardioli, P.W.4    Giordano, R.L.C.5
  • 40
    • 0024675074 scopus 로고
    • Immobilization-stabilization of enzymes; variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multipoint attachment
    • Blanco R.M., Calvete J.J., Guisán J.M. Immobilization-stabilization of enzymes; variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multipoint attachment. Enzyme Microb. Technol. 1989, 11:353-359.
    • (1989) Enzyme Microb. Technol. , vol.11 , pp. 353-359
    • Blanco, R.M.1    Calvete, J.J.2    Guisán, J.M.3
  • 41
    • 0344153356 scopus 로고    scopus 로고
    • Lactose hydrolysis by Lactozym™ immobilized on cellulose beds in batch and fluidized bed modes
    • Roy I., Gupta M.N. Lactose hydrolysis by Lactozym™ immobilized on cellulose beds in batch and fluidized bed modes. Process Biochem. 2003, 39:325-332.
    • (2003) Process Biochem. , vol.39 , pp. 325-332
    • Roy, I.1    Gupta, M.N.2
  • 42
    • 49149102826 scopus 로고    scopus 로고
    • Immobilization of β-galactosidase from K. lactis onto a polysiloxane-polyvinyl alcohol magnetic (mPOS-PVA) composite for lactose hydrolysis
    • Neri D.F.M., Balcão V.M., Carneiro-da-Cunha M.G., Carvalho L.B., Teixeira J.A. Immobilization of β-galactosidase from K. lactis onto a polysiloxane-polyvinyl alcohol magnetic (mPOS-PVA) composite for lactose hydrolysis. Catal. Commun. 2008, 9:2334-2339.
    • (2008) Catal. Commun. , vol.9 , pp. 2334-2339
    • Neri, D.F.M.1    Balcão, V.M.2    Carneiro-da-Cunha, M.G.3    Carvalho, L.B.4    Teixeira, J.A.5
  • 43
    • 73649143906 scopus 로고    scopus 로고
    • Cell disruption optimization and covalent immobilization of β-d-galactosidase from Kluyveromyces marxianus YW-1 for lactose hydrolysis in milk
    • Puri M., Gupta S., Pahuja P., Kaur A., Kanwar J.R., Kennedy J.F. Cell disruption optimization and covalent immobilization of β-d-galactosidase from Kluyveromyces marxianus YW-1 for lactose hydrolysis in milk. Appl. Biochem. Biotechnol. 2010, 160:98-108.
    • (2010) Appl. Biochem. Biotechnol. , vol.160 , pp. 98-108
    • Puri, M.1    Gupta, S.2    Pahuja, P.3    Kaur, A.4    Kanwar, J.R.5    Kennedy, J.F.6
  • 44
    • 75149156955 scopus 로고    scopus 로고
    • Lactose hydrolysis by β-galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode
    • Ansari S.A., Husain Q. Lactose hydrolysis by β-galactosidase immobilized on concanavalin A-cellulose in batch and continuous mode. J. Mol. Catal. B: Enzym. 2010, 63:68-74.
    • (2010) J. Mol. Catal. B: Enzym. , vol.63 , pp. 68-74
    • Ansari, S.A.1    Husain, Q.2
  • 45
    • 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
  • 46
    • 0019037829 scopus 로고
    • Immobilization of enzymes on chitin and chitosan
    • Muzzarelli R.A.A. Immobilization of enzymes on chitin and chitosan. Enzyme Microb. Technol. 1980, 2:177-184.
    • (1980) Enzyme Microb. Technol. , vol.2 , pp. 177-184
    • Muzzarelli, R.A.A.1
  • 47
    • 29344453545 scopus 로고    scopus 로고
    • Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase
    • Guar R., Pant H., Jain R., Khare S.K. Galacto-oligosaccharide synthesis by immobilized Aspergillus oryzae β-galactosidase. Food Chem. 2006, 97:426-430.
    • (2006) Food Chem. , vol.97 , pp. 426-430
    • Guar, R.1    Pant, H.2    Jain, R.3    Khare, S.K.4
  • 48
    • 84864966807 scopus 로고    scopus 로고
    • Effect of the support size on the properties of β-galactosidase immobilized on chitosan: advantages and disadvantages of macro and nanoparticles
    • Klein M.P., Nunes M.R., Rodrigues R.C., Benvenutti E.V., Costa T.M.H., Hertz P.F., Ninow J.L. Effect of the support size on the properties of β-galactosidase immobilized on chitosan: advantages and disadvantages of macro and nanoparticles. Biomacromolecules 2012, 13:2456-2464.
    • (2012) Biomacromolecules , vol.13 , pp. 2456-2464
    • Klein, M.P.1    Nunes, M.R.2    Rodrigues, R.C.3    Benvenutti, E.V.4    Costa, T.M.H.5    Hertz, P.F.6    Ninow, J.L.7
  • 49
    • 84877006520 scopus 로고    scopus 로고
    • Kinetics of lactose conversion to galacto-oligosaccharides by β-galactosidase immobilized on PVDF membrane
    • Palai T., Bhattacharya P.K. Kinetics of lactose conversion to galacto-oligosaccharides by β-galactosidase immobilized on PVDF membrane. J. Biosci. Bioeng. 2013, 115:668-673.
    • (2013) J. Biosci. Bioeng. , vol.115 , pp. 668-673
    • Palai, T.1    Bhattacharya, P.K.2
  • 50
    • 21644461452 scopus 로고    scopus 로고
    • Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method
    • Alonso N., López-Gallego F., Betancor L., Hidalgo A., Mateo C., Guisan J.M. Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method. J. Mol. Catal. B: Enzym. 2005, 35:57-61.
    • (2005) J. Mol. Catal. B: Enzym. , vol.35 , pp. 57-61
    • Alonso, N.1    López-Gallego, F.2    Betancor, L.3    Hidalgo, A.4    Mateo, C.5    Guisan, J.M.6


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