메뉴 건너뛰기




Volumn 58-59, Issue 1, 2011, Pages 33-38

A comparison of the kinetic properties of free and immobilized Aspergillus oryzae β-galactosidase

Author keywords

galactosidase; Alginate; Glucose; Immobilized enzymes; Kinetic parameters; Lactose

Indexed keywords

ASPERGILLUS ORYZAE; BUFFER SOLUTIONS; COMPETITIVE INHIBITION; ENZYMATIC ACTIVITIES; FREE ENZYME; GALACTOSIDASES; GLUTARALDEHYDES; IMMOBILIZED ENZYME; KINETIC PROPERTIES; LACTOSE; LACTOSE HYDROLYSIS; MICHAELIS-MENTEN MODEL; PH RANGE; SUBSTRATE CONCENTRATIONS; SUBSTRATE TRANSFER;

EID: 80054830878     PISSN: 1369703X     EISSN: 1873295X     Source Type: Journal    
DOI: 10.1016/j.bej.2011.08.011     Document Type: Article
Times cited : (40)

References (48)
  • 2
    • 0344153356 scopus 로고    scopus 로고
    • Lactose hydrolysis by Lactosym TM immobilized on cellulose beads in batch and fluidized bed modes
    • Roy I., Gupta M.N. Lactose hydrolysis by Lactosym TM immobilized on cellulose beads in batch and fluidized bed modes. Process Biochemistry 2003, 39:325-332.
    • (2003) Process Biochemistry , vol.39 , pp. 325-332
    • Roy, I.1    Gupta, M.N.2
  • 3
    • 84957455425 scopus 로고    scopus 로고
    • Scientific opinion on lactose thresholds in lactose intolerance and galactosaemia
    • Scientific opinion on lactose thresholds in lactose intolerance and galactosaemia, EFSA Journal. 8 (9) (2010) 1777.
    • (2010) EFSA Journal. , vol.8 , Issue.9 , pp. 1777
  • 5
    • 0034333646 scopus 로고    scopus 로고
    • Hydrolysis of lactose in whey permeate by immobilized β-galactosidase from Kluyveromyces fragilis
    • Szczodrak J. Hydrolysis of lactose in whey permeate by immobilized β-galactosidase from Kluyveromyces fragilis. Journal of Molecular Catalysis B: Enzymatic 2000, 10:631-637.
    • (2000) Journal of Molecular Catalysis B: Enzymatic , vol.10 , pp. 631-637
    • Szczodrak, J.1
  • 6
    • 33947513910 scopus 로고    scopus 로고
    • Calcium alginate entrapped preparation of A. oryzae β-galactosidase: its stability and applications in the hydrolysis of lactose
    • Haider T., Hussain Q. Calcium alginate entrapped preparation of A. oryzae β-galactosidase: its stability and applications in the hydrolysis of lactose. International Journal of Biological Macromolecules 2007, 41:72-80.
    • (2007) International Journal of Biological Macromolecules , vol.41 , pp. 72-80
    • Haider, T.1    Hussain, Q.2
  • 8
    • 13244292422 scopus 로고    scopus 로고
    • Effects of internal mass transfer and product inhibition on a simulated immobilized enzyme-catalyzed reactor for lactose hydrolysis
    • Al-Muftah A.E., Abu-Reesh I.M. Effects of internal mass transfer and product inhibition on a simulated immobilized enzyme-catalyzed reactor for lactose hydrolysis. Biochemical Engineering Journal 2005, 23:139-153.
    • (2005) Biochemical Engineering Journal , vol.23 , pp. 139-153
    • Al-Muftah, A.E.1    Abu-Reesh, I.M.2
  • 9
    • 40449132498 scopus 로고    scopus 로고
    • Perspectives and applications of immobilised β-galactosidase in food industry - a review
    • Grosová Z., Rosenberg M., Rebros M. Perspectives and applications of immobilised β-galactosidase in food industry - a review. Czech Journal of Food Sciences 2008, 26(1):1-14.
    • (2008) Czech Journal of Food Sciences , vol.26 , Issue.1 , pp. 1-14
    • Grosová, Z.1    Rosenberg, M.2    Rebros, M.3
  • 10
    • 0003206797 scopus 로고
    • Immobilisation of lactase (β-galactosidase) for use in dairy processing: a review
    • (Fevereiro/Março)
    • Greenberg N.A., Mahoney R.R. Immobilisation of lactase (β-galactosidase) for use in dairy processing: a review. Process Biochemistry 1981, (Fevereiro/Março).
    • (1981) Process Biochemistry
    • Greenberg, N.A.1    Mahoney, R.R.2
  • 14
    • 0034333338 scopus 로고    scopus 로고
    • Kinectic modeling of lactose hydrolysis with an immobilized β-galactosidase from Kluyveromyces fragilis
    • Ladero M., Santos A., García-Ocha F. Kinectic modeling of lactose hydrolysis with an immobilized β-galactosidase from Kluyveromyces fragilis. Enzyme and Microbial Technology 2000, 27:583-592.
    • (2000) Enzyme and Microbial Technology , vol.27 , pp. 583-592
    • Ladero, M.1    Santos, A.2    García-Ocha, F.3
  • 15
    • 80054843338 scopus 로고    scopus 로고
    • Immobilization of A. oryzae β-galactosidase ion exchange resins by combined ionic-binding method and cross-linking
    • Ansari S.A., Hussain Q. Immobilization of A. oryzae β-galactosidase ion exchange resins by combined ionic-binding method and cross-linking. Journal of Molecular Catalysis B: Enzymatic 2010, 63:93-101.
    • (2010) Journal of Molecular Catalysis B: Enzymatic , vol.63 , pp. 93-101
    • Ansari, S.A.1    Hussain, Q.2
  • 16
    • 77957936436 scopus 로고    scopus 로고
    • Immobilization of A. oryzae β-galactosidase in ion exchange resins by combined ionic-binding method and cross-linking
    • Guidini C.Z., Fisher J., Santana L.N.S., Cardoso V.L., Ribeiro E.J. Immobilization of A. oryzae β-galactosidase in ion exchange resins by combined ionic-binding method and cross-linking. Biochemical Engineering Journal 2010, 52:137-143.
    • (2010) Biochemical Engineering Journal , vol.52 , pp. 137-143
    • Guidini, C.Z.1    Fisher, J.2    Santana, L.N.S.3    Cardoso, V.L.4    Ribeiro, E.J.5
  • 19
    • 75149149796 scopus 로고    scopus 로고
    • Evaluation of the potential of polymeric carriers based on photo-crosslinkable chitosan in the formulation of lipase from Candida rugosa immobilization
    • Monier M., Wei Y., Sarhan A.A. Evaluation of the potential of polymeric carriers based on photo-crosslinkable chitosan in the formulation of lipase from Candida rugosa immobilization. Journal of Molecular Catalysis B: Enzymatic 2010, 63:93-101.
    • (2010) Journal of Molecular Catalysis B: Enzymatic , vol.63 , pp. 93-101
    • Monier, M.1    Wei, Y.2    Sarhan, A.A.3
  • 22
    • 16244405562 scopus 로고    scopus 로고
    • Immobilised enzymes: science or art?
    • Cao L. Immobilised enzymes: science or art?. Current Opinion in Chemical Biology 2005, 9:217-226.
    • (2005) Current Opinion in Chemical Biology , vol.9 , pp. 217-226
    • Cao, L.1
  • 25
    • 77952585408 scopus 로고    scopus 로고
    • Performance of β-galactosidase pretreated with lactose to prevent activity loss during the enzyme immobilisation process
    • Song Y.S., Lee J.H., Kang S.W., Kim S.W. Performance of β-galactosidase pretreated with lactose to prevent activity loss during the enzyme immobilisation process. Food Chemistry 2010, 123:1-5.
    • (2010) Food Chemistry , vol.123 , pp. 1-5
    • Song, Y.S.1    Lee, J.H.2    Kang, S.W.3    Kim, S.W.4
  • 26
    • 0030961569 scopus 로고    scopus 로고
    • A new method for immobilization of β-galactosidase and ist utilization in a plug flow reactor
    • Ates S., Mehmetoglu ü. A new method for immobilization of β-galactosidase and ist utilization in a plug flow reactor. Process Biochemistry 1997, 32:433-436.
    • (1997) Process Biochemistry , vol.32 , pp. 433-436
    • Ates, S.1    Mehmetoglu, Ü.2
  • 27
    • 0036739268 scopus 로고    scopus 로고
    • A novel method for the immobilization of de β-galactosidase
    • Tanriseven A.S., Dogan E. A novel method for the immobilization of de β-galactosidase. Process Biochesmitry 2002, 38:27-30.
    • (2002) Process Biochesmitry , vol.38 , pp. 27-30
    • Tanriseven, A.S.1    Dogan, E.2
  • 28
    • 72449172485 scopus 로고    scopus 로고
    • Characterization of galactosyl derivatives obtained by transgalactosylation of lactose and different polyols using immobilized beta-galactosidase from A. oryzae
    • Irazoqui G., Giacomina C., Batista-Viera F., Brena B.M., Cardelle-Cobas A., Corzo N., Jimeno M.L. Characterization of galactosyl derivatives obtained by transgalactosylation of lactose and different polyols using immobilized beta-galactosidase from A. oryzae. Journal of Agricultural and Food Chemistry 2009, 57:11302-11307.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 11302-11307
    • Irazoqui, G.1    Giacomina, C.2    Batista-Viera, F.3    Brena, B.M.4    Cardelle-Cobas, A.5    Corzo, N.6    Jimeno, M.L.7
  • 29
    • 35048822971 scopus 로고    scopus 로고
    • Elucidation of the mechanism and end products of glutaraldehyde crosslinking reaction by X-ray structure analysis
    • Wine Y., Cohen-Hadar N., Freeman A., Frolow F. Elucidation of the mechanism and end products of glutaraldehyde crosslinking reaction by X-ray structure analysis. Biotechnology and Bioengineering 2007, 98(3):711-718.
    • (2007) Biotechnology and Bioengineering , vol.98 , Issue.3 , pp. 711-718
    • Wine, Y.1    Cohen-Hadar, N.2    Freeman, A.3    Frolow, F.4
  • 34
    • 63749119165 scopus 로고    scopus 로고
    • Optimal immobilization of β-galactosidase from pea (PsBGAL) onto sephadex and chitosan beads using response surface methodology and its applications
    • Dwevedi A., Kayastha A.M. Optimal immobilization of β-galactosidase from pea (PsBGAL) onto sephadex and chitosan beads using response surface methodology and its applications. Bioresource Technology 2009, 100:2667-2675.
    • (2009) Bioresource Technology , vol.100 , pp. 2667-2675
    • Dwevedi, A.1    Kayastha, A.M.2
  • 35
    • 0032524182 scopus 로고    scopus 로고
    • Kinectic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromyces fragilis
    • Ladero M., Santos A., García-Ocha F. Kinectic modeling of lactose hydrolysis by a β-galactosidase from Kluyveromyces fragilis. Enzyme and Microbial Technology 1998, 22:558-567.
    • (1998) Enzyme and Microbial Technology , vol.22 , pp. 558-567
    • Ladero, M.1    Santos, A.2    García-Ocha, F.3
  • 37
    • 31844453423 scopus 로고    scopus 로고
    • Polyacrylamide-gelatine carrier system used for invertase immobilization
    • Emregul E., Sungur S., Akbulut U. Polyacrylamide-gelatine carrier system used for invertase immobilization. Food Chemistry 2006, 97:591-597.
    • (2006) Food Chemistry , vol.97 , pp. 591-597
    • Emregul, E.1    Sungur, S.2    Akbulut, U.3
  • 38
    • 30344475818 scopus 로고    scopus 로고
    • A novel approach to develop β-galactosidase entrapped in liposomes in order to prevent an immediate hydrolysis of lactose in milk
    • Nogales J.M.R., López A.D. A novel approach to develop β-galactosidase entrapped in liposomes in order to prevent an immediate hydrolysis of lactose in milk. International Dairy Journal 2006, 16:354-360.
    • (2006) International Dairy Journal , vol.16 , pp. 354-360
    • Nogales, J.M.R.1    López, A.D.2
  • 39
    • 9644299768 scopus 로고    scopus 로고
    • Soymilk oligosaccharide hydrolysis by A. oryzae α-galactosidase immobilized in calcium alginate
    • Prashanth S.J., Mulimani V.H. Soymilk oligosaccharide hydrolysis by A. oryzae α-galactosidase immobilized in calcium alginate. Process Biochemistry 2005, 40:1199-1205.
    • (2005) Process Biochemistry , vol.40 , pp. 1199-1205
    • Prashanth, S.J.1    Mulimani, V.H.2
  • 40
    • 29344453545 scopus 로고    scopus 로고
    • Galacto-oligosaccharide by immobilized A. oryzae β-galactosidase
    • Gaur R., Pant H., Jain R., Khare S.K. Galacto-oligosaccharide by immobilized A. oryzae β-galactosidase. Food Chemistry 2006, 97:426-430.
    • (2006) Food Chemistry , vol.97 , pp. 426-430
    • Gaur, R.1    Pant, H.2    Jain, R.3    Khare, S.K.4
  • 41
    • 0034748951 scopus 로고    scopus 로고
    • Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis
    • Zhou Q.Z.K., Chen X.D. Effects of temperature and pH on the catalytic activity of the immobilized β-galactosidase from Kluyveromyces lactis. Biochemical Engineering Journal 2001, 9:33-40.
    • (2001) Biochemical Engineering Journal , vol.9 , pp. 33-40
    • Zhou, Q.Z.K.1    Chen, X.D.2
  • 43
    • 33747097811 scopus 로고    scopus 로고
    • Chemically surface modified gel (CSMG): an excellent enzyme-immobilization matrix for industrial processes
    • David A.E., Wang N.S., Yang V.C., Yang A.J. Chemically surface modified gel (CSMG): an excellent enzyme-immobilization matrix for industrial processes. Journal of Biotechnology 2006, 125:395-407.
    • (2006) Journal of Biotechnology , vol.125 , pp. 395-407
    • David, A.E.1    Wang, N.S.2    Yang, V.C.3    Yang, A.J.4
  • 44
    • 34249077182 scopus 로고    scopus 로고
    • Immobilization of α-amylase on zirconia: a heterogeneous biocatalyst for starch hydrolysis
    • Reshmi R., Sanjay G., Sugunan S. Immobilization of α-amylase on zirconia: a heterogeneous biocatalyst for starch hydrolysis. Catalysis Communications 2007, 8:393-399.
    • (2007) Catalysis Communications , vol.8 , pp. 393-399
    • Reshmi, R.1    Sanjay, G.2    Sugunan, S.3
  • 45
    • 4043069789 scopus 로고    scopus 로고
    • Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition promoted by glucose. Full hydrolysis of lactose in milk
    • Mateo C., Monti R., Pessela B.C.C., Fuentes M., Torres R., Guisán J.M., Fernández-Lafuente R. Immobilization of lactase from Kluyveromyces lactis greatly reduces the inhibition promoted by glucose. Full hydrolysis of lactose in milk. Biotechnology Progress 2004, 20:1259-1262.
    • (2004) Biotechnology Progress , vol.20 , pp. 1259-1262
    • Mateo, C.1    Monti, R.2    Pessela, B.C.C.3    Fuentes, M.4    Torres, R.5    Guisán, J.M.6    Fernández-Lafuente, R.7
  • 48
    • 79953315791 scopus 로고    scopus 로고
    • Determination of the transgalactosylation activity of A. oryzae β-galactosidase: effect of pH, temperature and galactose and glucose concentrations
    • Vera C., Guerrero C., Illanes A. Determination of the transgalactosylation activity of A. oryzae β-galactosidase: effect of pH, temperature and galactose and glucose concentrations. Carbohydrate Research 2011, 346(6):745-752.
    • (2011) Carbohydrate Research , vol.346 , Issue.6 , pp. 745-752
    • Vera, C.1    Guerrero, C.2    Illanes, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.