Amino acid modified chitosan beads: Improved polymer supports for immobilization of lipase from Candida rugosa

Journal of Molecular Catalysis B: Enzymatic

Volumn 57, Issue 1-4, 2009, Pages 123-129

  Yi, Song Se ^a   Noh, Jin Mi ^a   Lee, Yoon Sik ^a  

^a Seoul National University   (South Korea)

Author keywords

Activity; Amino acid; Chitosan bead; Enzyme immobilization; Epichlorohydrin; Lipase; Thermal stability

Indexed keywords

ACTIVITY; CANDIDA RUGOSA; CHITOSAN BEAD; CHITOSAN BEADS; ELEMENTAL ANALYSIS; EPICHLOROHYDRIN; IMMOBILIZED LIPASE; INITIAL ACTIVITY; KINETIC DATA; LIPASE FROM CANDIDA RUGOSA; MODIFIED CHITOSAN; POLYMER SUPPORTS; SOLID STATE NMR; SUBSTRATE SPECIFICITY; THERMAL STABILITY;

AMINATION; AMINO ACIDS; CHITIN; CHITOSAN; ELECTRIC CIRCUIT BREAKERS; ENZYMES; LIPASES; ORGANIC ACIDS; THERMODYNAMIC STABILITY;

ENZYME IMMOBILIZATION;

AMINO ACID; CHITOSAN; EPICHLOROHYDRIN; TRIACYLGLYCEROL LIPASE;

ARTICLE; CANDIDA RUGOSA; CHEMICAL ANALYSIS; CHEMICAL MODIFICATION; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME IMMOBILIZATION; ENZYME KINETICS; ENZYME SPECIFICITY; ENZYME STABILITY; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; STORAGE TEMPERATURE; THERMOSTABILITY;

CANDIDA RUGOSA;

EID: 67651028314     PISSN: 13811177     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcatb.2008.08.002     Document Type: Article

References (47)

1. Polaina P., and MacCabe A.P. Industrial Enzymes: Structure, Function and Applications (2007), Springer, Dordrecht, The Netherland
2. Buchholz K., Kasche V., and Bornscheuer U.T. Biocatalysts and Enzyme Technology (2005), Wiley-VCH Verlag GmbH, Weinheim
3. Woolley P., and Petersen S.B. Lipases: their Structure Biochemistry and Application (1994), Cambridge University Press
4. Woodley J.M. Solid Supports Catal. Org. Synth. 71 (1992) 254-271
5. Balcâo V.M., Paiva A.L., and Malcata F.X. Enzyme Microb. Technol. 18 (1996) 392-416
6. de Lathouder K.M., van Benthem D.T.J., Wallin S.A., Mateo C., Fernandez Lafuente F., Guisan J.M., Kapteijn F., and Moulijn J.A. J. Mol. Catal. B-Enzym. 50 (2008) 20-27
7. Ravi Kumar M.N.V., Muzzarelli R.A.A., Muzzarelli C., Sashiwa H., and Domb A.J. Chem. Rev. 104 (2004) 6017-6084
8. Krajewska B. Enzyme Microb. Technol. 35 (2004) 126-139
9. Dinçer A., and Telefoncu A. J. Mol. Catal. B-Enzym. 45 (2007) 10-14
10. Altun G.D., and Centinus S.A. Food Chem. 100 (2007) 964-971
11. Yi S.S., Lee C., Kim J., Kyung D., Kim B.G., and Lee Y.S. Process Biochem. 42 (2007) 895-898
12. Chiou S.H., and Wu W.T. Biomaterials 25 (2004) 197-204
13. Kilinç A., Teke M., Önal S., and Telefoncu A. Prep. Biochem. Biotechnol. 36 (2006) 153-163
14. Hung T.C., Giridhar R., Chiou S.H., and Wu W.T. J. Mol. Catal. B-Enzym. 26 (2003) 69-78
15. Itoyama K., Tokura S., and Hayashi T. Biotechnol. Prog. 10 (1994) 225-229
16. Ye P., Xu J.K., Che A.F., Wu J., and Seta P. Biomaterials 26 (2005) 6394-6403
17. Ye P., Xu J.K., Wu J., Innocent C., and Seta P. Biomaterials 27 (2006) 4169-4176
18. Huang X.J., Ge D., and Xu Z.K. Eur. Polym. J. 51 (2007) 3710-3718
19. Tang Z.X., Qian J.Q., and Shi L.E. Mater. Lett. 61 (2007) 37-40
20. Chiou S.H., Hung T.C., Giridhar R., and Wu W.T. Prep. Biochem. Biotech. 37 (2007) 265-275
21. Rodrigues D.S., Mendes A.A., Adriano W.S., Gonçalves L.R.B., and Giordano R.L.C. J. Mol. Catal. B-Enzym. 51 (2008) 100-109
22. Tan T., Wang F., and Zhang H. J. Mol. Catal. B-Enzym. 18 (2002) 325-331
23. Doellgast G.J., and Plaut A.G. Immunochemistry 13 (1976) 135-139
24. Kim M., Furusaki S., Sato T., Sugo T., Ishigaki I., and Saito K. J. Chromatogr. 585 (1991) 45-51
25. Kim M., Furusaki S., Sugo T., Ishigaki I., and Saito K. J. Chromatogr. 586 (1991) 27-33
26. Kiyohara S., Sasaki M., Saito K., Sugita K., and Sugo T. J. Membr. Sci. 109 (1996) 87-92
27. Zeng X., and Ruckesteine E. Ind. Eng. Chem. Res. 35 (1996) 4169-4175
28. Subramanian A., Rau A.V., and Kaligotla H. Carbohydr. Polym. 66 (2006) 321-332
29. Scoble J.A., and Scopes R.K. J. Chromatogr. A 752 (1996) 67-76
30. Bradford M. Anal. Biochem. 72 (1976) 248-254
31. Winkler U.K., and Stuckmann M. J. Bacteriol. 138 (1979) 663-670
32. Gupta N., Rathi P., and Gupta R. Anal. Biochem. 311 (2002) 98-99
33. Brady L., Brzozowski A.M., Derewenda Z.S., Dodson E., Dodson G., Tolley S., Turkenburg J.P., Christiansen L., Huge-Jensen B., Norskov L., Thim L., and Menge U. Nature 343 (1990) 767-770
34. Derewenda U., Brzozowski A.M., Lawson D.M., and Derewenda Z.S. Biochemistry 31 (1992) 1532-1541
35. Ferandez-Lafuente R., Aemisén P., Sabuquillo P., Fernández-Lorente G., and Guisán J.M. Chem. Phys. Lipids 93 (1998) 185-197
36. Palomo J.M., Muñoz G., Fernández-Lorente G., Mateo C., Fernández-Lafuente R., and Guisán J.M. J. Mol. Catal. B-Enzym. 279 (2002) 19-20
37. Bastida A., Sabuquillo P., Armisen P., Fernández-Lafuente R., Huguet J., and Guisán J.M. Biotechnol. Bioeng. 58 (1998) 486-493
38. Gomes F.M., Pereira E.B., and de Castro H.F. Biomacromolecules 5 (2004) 17-23
39. Krajewska B., and Piwowarska Z. Biocatal. Biotransform. 23 (2005) 225-232
40. Vaillant F., Millan A., Millan P., Dornier M., Decloux M., and Reynes M. Process Biochem. 35 (2000) 989-996
41. Wyss A., von Stockar U., and Marison I.W. Biotechnol. Bioeng. 93 (2006) 28-39
42. Shaw J.F., Chang R.C., Wang F.F., and Wang Y.J. Biotechnol. Bioeng. 35 (1990) 132-137
43. Perez V.H., da Silva G.S., Gomes F.M., and de Castro H.F. Biochem. Eng. J. 34 (2007) 13-19
44. Ye P., Jiang J., and Xu Z.K. Colloid Surf. B-Biointerfaces 60 (2007) 62-67
45. dos Prazeres J.N., Cruz J.A.B., and Pastore G.M. Braz. J. Microbiol. 37 (2006) 505-509
46. Martin J.C., Bello J.F., Burguillo F.J., and Roig M.G. J. Mol. Catal. 93 (1994) 37-52
47. Paiva A.L., Balcão V.N., and Malcata F.X. Enzyme Microb. Technol. 27 (2000) 187-204