메뉴 건너뛰기




Volumn 39, Issue 4, 2011, Pages 259-266

Immobilization of β-galactosidase on novel polymers having Schiff bases

Author keywords

galactosidase; Immobilization; Lineweaver Burk plot; Polymeric support; Schiff bases; Storage capacity

Indexed keywords

GALACTOSIDASES; LINEWEAVER-BURK PLOTS; POLYMERIC SUPPORTS; SCHIFF BASIS; STORAGE CAPACITY;

EID: 79959929015     PISSN: 10731199     EISSN: 15324184     Source Type: Journal    
DOI: 10.3109/10731199.2011.555837     Document Type: Article
Times cited : (16)

References (33)
  • 1
    • 0015909646 scopus 로고
    • The purifi cation and properties of β-galactosidase from bovine testes
    • Distler, J.J., Jourdian, G.W. (1973). The purifi cation and properties of β-galactosidase from bovine testes. J Biol Chem. 248: 6772-6780.
    • (1973) J Biol Chem , vol.248 , pp. 6772-6780
    • Distler, J.J.1    Jourdian, G.W.2
  • 2
    • 0036010270 scopus 로고    scopus 로고
    • Immobilization of β-galactosidase on fibrous matrix by polyethyleneimine for production of galacto-oligosaccharides from lactose
    • DOI 10.1021/bp010167b
    • Albayrak, N., Yang, S.-T. (2002). Immobilization of β-galactosidase on fi brous matrix by polyethyleneimine for production of galacto- oligosaccharides from lactose. Biotechnology Progress. 18: 240-251. (Pubitemid 34294232)
    • (2002) Biotechnology Progress , vol.18 , Issue.2 , pp. 240-251
    • Albayrak, N.1    Yang, S.-T.2
  • 3
    • 75749118477 scopus 로고    scopus 로고
    • Stabilities of immobilized b-galactosidase of aspergillus sp. AF for the optimal produhction of galactooligosaccharides from lactose
    • Feng, Y., Chang, X., Wang, W., Ma, R. (2010). Stabilities of immobilized b-galactosidase of aspergillus sp. AF for the optimal production of galactooligosaccharides from lactose. Artificial Cells, Blood Substitutes, and Biotechnology. 38: 43-51.
    • (2010) Artificial Cells, Blood Substitutes, and Biotechnology , vol.38 , pp. 43-51
    • Feng, Y.1    Chang, X.2    Wang, W.3    Ma, R.4
  • 5
    • 0001448531 scopus 로고
    • Puri fi cation and properties of β-galactosidase from Bacillus circulans
    • Mozaffer, Z., Nakanishi, K., Matsuno, R., Kamikubo, T. (1984). Puri fi cation and properties of β-galactosidase from Bacillus circulans. Agric. Biol. Chem. 48: 3053-3061.
    • (1984) Agric. Biol. Chem , vol.48 , pp. 3053-3061
    • Mozaffer, Z.1    Nakanishi, K.2    Matsuno, R.3    Kamikubo, T.4
  • 6
    • 0036739268 scopus 로고    scopus 로고
    • A novel method for the immobilization of β-galactosidase
    • Tanriseven, A., Doǧan, S. (2002). A novel method for the immobilization of β-galactosidase. Process Biochemistry. 38: 27-30.
    • (2002) Process Biochemistry , vol.38 , pp. 27-30
    • Tanriseven, A.1    Doǧan, S.2
  • 7
    • 0343807464 scopus 로고    scopus 로고
    • Immobilization of β-galactosidase on graphite surface by glutaraldehyde
    • DOI 10.1016/S0260-8774(00)00147-3
    • Zhou, Q. Z. K., Chen, X. D. (2001). Immobilization of β-galactosidase on graphite surface by glutaraldehyde. Journal of Food Engineering; 48: 69-74. (Pubitemid 32034652)
    • (2001) Journal of Food Engineering , vol.48 , Issue.1 , pp. 69-74
    • Zhou, Q.Z.K.1    Dong Chen, X.2
  • 8
    • 0003969909 scopus 로고
    • Immobilization of yeast by invertase adsorpstion on magnetite
    • Kubal, B.S., Sankaran, K., DSouza, S.F. (1989). Immobilization of yeast by invertase adsorpstion on magnetite. J Microb Biotechnol. 4: 98-102.
    • (1989) J Microb Biotechnol , vol.4 , pp. 98-102
    • Kubal, B.S.1    Sankaran, K.2    Dsouza, S.F.3
  • 10
    • 0023138091 scopus 로고
    • Invertase immobilized on macroporous polystyrene: Properties and kinetic characterization
    • DOI 10.1002/bit.260290111
    • Mansfeld, A., Schellenberger, A. (1987). Invertase immobilized on macroporous polystyrene: Propeties and kinetic characterization. Biotechnol Bioeng. 29: 72-78. (Pubitemid 17059298)
    • (1987) Biotechnology and Bioengineering , vol.29 , Issue.1 , pp. 72-78
    • Mansfeld, J.1    Schellenberger, A.2
  • 11
    • 42749086539 scopus 로고    scopus 로고
    • Immobilization of invertase onto poly(3-methylthienyl methacrylate)/poly(3-thiopheneacetic acid) matrix
    • Dizge, N., Gunaydin, O., Yilmaz, F., Tanriseven, A. (2008). Immobilization of invertase onto poly(3-methylthienyl methacrylate)/poly(3- thiopheneacetic acid) matrix. Biochem Eng J. 40: 64-71.
    • (2008) Biochem Eng J , vol.40 , pp. 64-71
    • Dizge, N.1    Gunaydin, O.2    Yilmaz, F.3    Tanriseven, A.4
  • 12
    • 12344312508 scopus 로고    scopus 로고
    • Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports
    • DOI 10.1016/j.jbiotec.2004.09.015, PII S0168165604005073
    • Lopez-Gallego, F., Montes, T., Fuentes, M., Alons,o N., Grazu, V., Betancor, L., Guisan, J.M., Fernandez-Lafuente, R. (2005). Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl suppports. J Biotechnol. 116: 1-10. (Pubitemid 40126162)
    • (2005) Journal of Biotechnology , vol.116 , Issue.1 , pp. 1-10
    • Lopez-Gallego, F.1    Montes, T.2    Fuentes, M.3    Alonso, N.4    Grazu, V.5    Betancor, L.6    Guisan, J.M.7    Fernandez-Lafuente, R.8
  • 13
    • 0024677047 scopus 로고
    • Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels. Borohydride reduction of trypsin-agarose derivatives
    • DOI 10.1016/0141-0229(89)90020-3
    • Blanco, R.M., Guisan, J.M. (1988). Stabilization of enzymes by multipoint covalent attachment to agarose-aldehyde gels: Borohydre reduction of trypsin-agarose derivatives. Enzyme Microb Technol. 11: 360-366. (Pubitemid 19138659)
    • (1989) Enzyme and Microbial Technology , vol.11 , Issue.6 , pp. 360-366
    • Blanco, R.M.1    Guisan, J.M.2
  • 14
    • 0026417558 scopus 로고
    • Immobilization-stabilization of chymotrypsin by covalent attachment to aldehyde agarose gels
    • Guisan, J.M., Bastida, A., Cuesta, C., Fernandez-Lafuante, R., Rosell, C.M. (1991). Immobilization-stabilization of chymotrypsin by covalent attachment to aldehyde agarose gels. Biotechnol Bioeng. 9: 75-84.
    • (1991) Biotechnol Bioeng , vol.9 , pp. 75-84
    • Guisan, J.M.1    Bastida, A.2    Cuesta, C.3    Fernandez-Lafuante, R.4    Rosell, C.M.5
  • 15
    • 0034111128 scopus 로고    scopus 로고
    • Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment
    • DOI 10.1016/S0141-0229(99)00188-X, PII S014102299900188X
    • Mateo, C., Abian, O., Fernandez-Lafuante, R., Guisan, J.M. (2000). Increase in conformational stability of enzymes immobilized on epoxy-activated supports by favoring additional multipoint covalent attachment. Enzyme and Microbial Technology. 26: 509-515. (Pubitemid 30193324)
    • (2000) Enzyme and Microbial Technology , vol.26 , Issue.7 , pp. 509-515
    • Mateo, C.1    Abian, O.2    Fernandez-Lafuente, R.3    Guisan, J.M.4
  • 16
    • 21644461452 scopus 로고    scopus 로고
    • Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method
    • DOI 10.1016/j.molcatb.2005.05.007, PII S1381117705000822
    • Alonso, N., Lopez-Gallego, F., Betancor, L., Hidalgo, A., Mateo, C., Guisan, J.M. Fernandez-Lafuente, R. (2005). Immobilization and stabilization of glutaryl acylase on aminated sepabeads supports by the glutaraldehyde crosslinking method. Journal of Moleculer Catalysis B: Enzymatic. 35: 57-61. (Pubitemid 40933749)
    • (2005) Journal of Molecular Catalysis B: Enzymatic , vol.35 , Issue.1-3 , pp. 57-61
    • Alonso, N.1    Lopez-Gallego, F.2    Betancor, L.3    Hidalgo, A.4    Mateo, C.5    Guisan, J.M.6    Fernandez-Lafuente, R.7
  • 18
    • 18844407761 scopus 로고    scopus 로고
    • Oxidation of limonene over carbon anchored transition metal Schiff base complexes: Effect of the linking agent
    • DOI 10.1016/j.cattod.2005.02.034, PII S0920586105000295, 1st International Symposium on Carbon for Catalysis CARBOCAT-1
    • Oliveira, P., Ramos, A.M., Fonseca, I., Botelho Do Rego, A., Vital, J. (2005). Oxidation of limonene over carbon anchored transition metal Schiff base complexes: Effect of the linking agent. Catal Today. 102-103: 67-77. (Pubitemid 40683976)
    • (2005) Catalysis Today , vol.102-103 , pp. 67-77
    • Oliveira, P.1    Ramos, A.M.2    Fonseca, I.3    Botelho Do Rego, A.4    Vital, J.5
  • 19
    • 33846804397 scopus 로고    scopus 로고
    • Removal of Fe(III) using a polystyrene anchored schiff base
    • DOI 10.1007/s10311-006-0070-1
    • Krishnapillai, G.K., Konnully, S.J. (2007). Removal of Fe(III) using polystyrene anchored Schiff base. Environ Chem Lett. 5: 19-21. (Pubitemid 46206419)
    • (2007) Environmental Chemistry Letters , vol.5 , Issue.1 , pp. 19-21
    • Krishnapillai, G.K.1    Konnully, S.J.2
  • 20
    • 0034684068 scopus 로고    scopus 로고
    • A highly selective synthesis of N-acetyllactosamine catalyzed by immobilised β-galactosidase from Bacillus circulans
    • DOI 10.1016/S1381-1177(99)00112-5, PII S1381117799001125
    • Hernaiz, M.J., Crout, H.G. (2000). A highly selective synthesis of N-acetyllactosamine catalyzed by immobilised β-galactosidase from Bacillus circulans. J Mol Catal B: Enzym. 10: 403-8. (Pubitemid 30483994)
    • (2000) Journal of Molecular Catalysis - B Enzymatic , vol.10 , Issue.4 , pp. 403-408
    • Hernaiz, M.J.1    Crout, D.H.G.2
  • 21
    • 33747849215 scopus 로고    scopus 로고
    • First example of schiff bases containing poly(acryl amid) in the synthesis and characterization
    • DOI 10.1080/10601320600897007, PII U2960407K75138K0
    • Sari, N. (2006). First example of Schiff bases containing poly(acryl amid) in the synthesis and characterization. J Macromol Sci Pure Appl Chem. 43: 1609-1618. (Pubitemid 44286089)
    • (2006) Journal of Macromolecular Science, Part A: Pure and Applied Chemistry , vol.43 , Issue.10 , pp. 1609-1618
    • Sari, N.1
  • 23
    • 70149104818 scopus 로고    scopus 로고
    • Synthesis, characterization, and selectivity studies of poly(acrylamide) incorporating Schiff bases
    • Sari , N., Özcan, Ö. (2009). Synthesis, characterization, and selectivity studies of poly(acrylamide) incorporating Schiff bases. Chinese Journal of Polymer Science. 27: 675-683.
    • (2009) Chinese Journal of Polymer Science , vol.27 , pp. 675-683
    • Sari, N.1    Özcan, Ö.2
  • 24
    • 35248836478 scopus 로고    scopus 로고
    • 3: A comparative study
    • DOI 10.1016/j.bej.2007.03.006, PII S1369703X07001313
    • Ghamgui, H., Miled, N., Karra-Chaabouni, M., Gargouri, Y. (2007). Immobilization studies and biochemical properties of free and immobilized Rhizopus oryzae lipase onto CaCO 3: A comparative study. Biochem Eng J. 37: 34-41. (Pubitemid 47559145)
    • (2007) Biochemical Engineering Journal , vol.37 , Issue.1 , pp. 34-41
    • Ghamgui, H.1    Miled, N.2    Karra-chaabouni, M.3    Gargouri, Y.4
  • 26
    • 0343293895 scopus 로고    scopus 로고
    • The effect of gel composition on the adsorption of invertase on poly(acrylamide/maleic acid) hydrogels
    • DOI 10.1016/S0956-7135(99)00114-0, PII S0956713599001140
    • Arslan, F., Tumturk, H., Caykara, T., Şen, M., Guven, O. (2000). The effect of gel composition on the adsorption of invertase on poly(acrylamide/maleic acid) hydrogels. Food Chem. 70: 33-38. (Pubitemid 30227579)
    • (2000) Food Chemistry , vol.70 , Issue.1 , pp. 33-38
    • Arslan, F.1    Tumturk, H.2    Caykara, T.3    Sen, M.4    Guven, O.5
  • 27
    • 74149093174 scopus 로고    scopus 로고
    • Immobilization of β-galactosidase on galactose-containing polymeric beads
    • Okutucu, B., Celem, E. B., ̈nal, S. (2010). Immobilization of β-galactosidase on galactose-containing polymeric beads. Enzyme Microb Tech. 46: 200-205.
    • (2010) Enzyme Microb Tech , vol.46 , pp. 200-205
    • Okutucu, B.1    Celem, E.B.2    Önal, S.3
  • 28
    • 0037207028 scopus 로고    scopus 로고
    • Enzymic degradation of raffinose family oligosaccharides in soymilk by immobilized α-galactosidase from Gibberella fujikuroi
    • DOI 10.1016/S0032-9592(02)00010-9, PII S0032959202000109
    • Thippeswamy, S., Mulimani, V.H. (2003), Enzymic degradation of raf fi nose family oligosaccharides in soymilk by immobilized β-galactosidase from Gibberella fujikuroi. Process Biochem. 38: 635-40. (Pubitemid 35404800)
    • (2002) Process Biochemistry , vol.38 , Issue.5 , pp. 635-640
    • Thippeswamy, S.1    Mulimani, V.H.2
  • 29
    • 33847166926 scopus 로고    scopus 로고
    • A new method for immobilization of acetylcholinesterase
    • DOI 10.1007/s00449-006-0106-8
    • Tumturk, H., Sahin, F., Demirel, G. (2007). A new method for immobilization of acetylcholinesterase. Bioproc Biosyst Eng. 30: 141-145. (Pubitemid 46295329)
    • (2007) Bioprocess and Biosystems Engineering , vol.30 , Issue.2 , pp. 141-145
    • Tumturk, H.1    Sahin, F.2    Demirel, G.3
  • 30
    • 58349088526 scopus 로고    scopus 로고
    • Functional poymeric supports for immobilization of cholesterol oxidase
    • Akkaya, B., Sahin, F., Demirel, G., Tumturk, H. (2009). Functional poymeric supports for immobilization of cholesterol oxidase. Biochem Eng J. 43: 333-337.
    • (2009) Biochem Eng J , vol.43 , pp. 333-337
    • Akkaya, B.1    Sahin, F.2    Demirel, G.3    Tumturk, H.4
  • 32
    • 33846850249 scopus 로고    scopus 로고
    • Preparation and application of poly(N,N-dimethylacrylamide-co-acrylamide) and poly(N-isopropylacrylamide-co-acrylamide)/κ-Carrageenan hydrogels for immobilization of lipase
    • DOI 10.1016/j.ijbiomac.2006.07.004, PII S0141813006002297
    • Tumturk, H., Karaca, N., Demirel, G., Şahin, F. (2007). Preparation and application of poly(N,N-dimethylacrylamide- co-acrylamide) and poly(N-isopropylacrylamide- co acrylamide)-Carrageenan hydrogels for immobilization of lipase. Int. J. Biol. Macromolecules. 40: 281-285. (Pubitemid 46215729)
    • (2007) International Journal of Biological Macromolecules , vol.40 , Issue.3 , pp. 281-285
    • Tumturk, H.1    Karaca, N.2    Demirel, G.3    Sahin, F.4
  • 33
    • 33947159656 scopus 로고    scopus 로고
    • Covalent immobilization of invertase on chemically activated poly(2-hydroxyethyl methacrylate) microbeads
    • Altinok, H., Aksoy, S., Tümtürk, H., Hasirci, N. (2006). Covalent immobilization of invertase on chemically activated poly(2-hydroxyethyl methacrylate) microbeads. Russian Chemical Bulletin, International Edition. 55: 1860-1864.
    • (2006) Russian Chemical Bulletin, International Edition , vol.55 , pp. 1860-1864
    • Altinok, H.1    Aksoy, S.2    Tümtürk, H.3    Hasirci, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.