The presence of thiolated compounds allows the immobilization of enzymes on glyoxyl agarose at mild pH values: New strategies of stabilization by multipoint covalent attachment

Enzyme and Microbial Technology

Volumn 45, Issue 6-7, 2009, Pages 477-483

  Bolivar, Juan M ^a   López Gallego, Fernando ^a   Godoy, Cesar ^a   Rodrigues, Dasciana S ^a,b   Rodrigues, Rafael C ^a   Batalla, Pilar ^a   Rocha Martín, Javier ^a   Mateo, Cesar ^a   Giordano, Raquel L C ^b   Guisán, José M ^a  

^a INSTITUTO DE CATÁLISIS Y PETROLEOQUÍMICA   (Spain)

^b FEDERAL UNIVERSITY OF SÃO CARLOS   (Brazil)

Author keywords

Enzyme immobilization; Enzyme stabilization; Glyoxyl; Imino bonds; Multipoint covalent attachment

Indexed keywords

AMINO GROUP; COVALENT ATTACHMENT; COVALENT REACTION; DENSE LAYER; DITHIOTHREITOL; ENZYME STABILIZATION; GLUTARYL ACYLASE; GLYOXYL; GLYOXYL AGAROSE; IMINO BONDS; IMMOBILIZED ENZYME; MULTIPOINT; MULTIPOINT COVALENT ATTACHMENT; NEW STRATEGY; PENICILLIN G ACYLASE; PH VALUE; PROTEIN SURFACE; PSEUDOMONAS SP; SODIUM BOROHYDRIDES; SOLUBLE ENZYMES;

ALDEHYDES; AMINATION; AMINES; BACTERIOLOGY; CATALYSTS; DIFFERENTIAL AMPLIFIERS; DRUG PRODUCTS; ENZYMES; ESCHERICHIA COLI; PH EFFECTS; PROGRAMMED CONTROL SYSTEMS; SODIUM; STABILIZATION;

ENZYME IMMOBILIZATION;

AGAROSE; ALDEHYDE DERIVATIVE; BACTERIAL ENZYME; DITHIOTHREITOL; GLUTARYL ACYLASE; LYSINE; PENICILLIN AMIDASE; SODIUM BOROHYDRIDE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

ARTICLE; BACILLUS; BACILLUS THERMOCATENULATUS; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; ENZYME IMMOBILIZATION; ENZYME MECHANISM; ENZYME STABILITY; ENZYME SYNTHESIS; ESCHERICHIA COLI; INCUBATION TIME; NONHUMAN; PH; PSEUDOMONAS; REDUCTION;

ESCHERICHIA COLI; GEOBACILLUS THERMOCATENULATUS; PSEUDOMONAS SP.;

EID: 70349783546     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2009.09.001     Document Type: Article

References (55)

1. Cao L. Immobilised enzymes: science or art?. Curr Opin Chem Biol 9 (2005) 217-226
2. Cao L., van Langen L., and Sheldon R.A. Immobilised enzymes: carrier-bound or carrier-free?. Curr Opin Biotechnol 14 (2003) 387-394
3. Sheldon R.A. Enzyme immobilization: the quest for optimum performance. Adv Synth Catal 349 (2007) 1289-1307
4. Mateo C., Palomo J.M., Fernandez-Lorente G., Guisan J.M., and Fernandez-Lafuente R. Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme Microb Technol 40 (2007) 1451-1463
5. Bolivar J.M., Wilson L., Ferrarotti S.A., Fernandez-Lafuente R., Guisan J.M., and Mateo C. Stabilization of a formate dehydrogenase by covalent immobilization on highly activated glyoxyl-agarose supports. Biomacromolecules 7 (2006) 669-673
6. Bolivar J.M., Wilson L., Ferrarotti A., Guisán S.J.M., Fernández-Lafuente R., and Mateo C. Improvement of the stability of alcohol dehydrogenase by covalent immobilization on glyoxyl-agarose. J Biotechnol 125 (2006) 85-94
7. Klibanov A.M. Enzyme stabilization by immobilization. Anal Biochem 93 (1979) 1-25
8. Gianfreda L., and Scarfi M.R. Enzyme stabilization: state of the art. Mol Cell Biochem 100 (1991) 97-128
9. Guisán J.M. Immobilization of enzymes and cells: methods in biotechnology (2006), Humana Press, Totowa, NJ, USA
10. Mateo C., Abian O., Bernedo M., Cuenca E., Fuentes M., Fernandez-Lorente G., et al. Some special features of glyoxyl supports to immobilize proteins. Enzyme Microb Technol 37 (2005) 456-462
11. Pedroche J., Yust M.M., Mateo C., Fernández-Lafuente R., Girón-Calle J., Alaiz M., et al. Effect of the support and experimental conditions in the intensity of the multipoint covalent attachment of proteins on glyoxyl-agarose supports: correlation between enzyme-support linkages and thermal stability. Enzyme Microb Technol 40 (2007) 1160-1167
12. Nilsson K., and Mosbach K. p-Toluenesulfonyl chloride as an activating agent of agarose for the preparation of immobilized affinity ligands and proteins. Eur J Biochem 112 (1980) 397-402
13. Albayrak N., and Yang S.-T. Immobilization of Aspergillus oryzae β-galactosidase on tosylated cotton cloth. Enzyme Microb Technol 31 (2002) 371-383
14. Migneault I., Dartiguenave C., Bertrand M.J., and Waldron K.C. Glutaraldehyde: behavior in aqueous solution, reaction with proteins, and application to enzyme crosslinking. BioTechniques 37 (2004) 790-802
15. Betancor L., López-Gallego F., Hidalgo A., Alonso-Morales N., Mateo G.D.-O.-C., Fernández-Lafuente R., et al. Different mechanisms of protein immobilization on glutaraldehyde activated supports: effect of support activation and immobilization conditions. Enzyme Microb Technol 39 (2006) 877-882
16. Schnapp J., and Shalitin Y. Immobilization of enzymes by covalent binding to amine supports via cyanogen bromide activation. Biochem Biophys Res Commun 70 (1976) 8-14
17. Jennissen H.P. Cyanogen bromide and tresyl chloride chemistry revisited: the special reactivity of agarose as a chromatographic and biomaterial support for immobilizing novel chemical groups. J Mol Recognit 8 (1995) 116-124
18. Blanco R.M., Calvete J.J., and Guisan J.M. Immobilization-stabilization of enzymes; variables that control the intensity of the trypsin (amine)-agarose (aldehyde) multipoint attachment. Enzyme Microb Technol 11 (1989) 353-359
19. Grazu V., Betancor L., Montes T., Lopez-Gallego F., Guisan J.M., and Fernandez-Lafuente R. Glyoxyl agarose as a new chromatographic matrix. Enzyme Microb Technol 38 (2006) 960-966
20. Mateo C., Palomo J.M., Fuentes M., Betancor L., Grazu V., Lopez-Gallego F., et al. Glyoxyl-agarose: a fully inert hydrophilic support for immobilization and high stabilization of proteins. Enzyme Microb Technol 39 (2006) 274-280
21. Mansfeld J., Vriend G., Vanden Burg B., Eijsink V., and Ulbrich-Hofmann R. Probing the unfolding region in a thermolysin-like protease by site-specific immobilization. Biochemistry 38 (1999) 8240-8245
22. Mansfeld J., and Ulbrich-Hofmann R. Site-specific and random immobilization of thermolysin-like proteases reflected in the thermal inactivation kinetics. Biotechnol Appl Biochem 32 (2000) 185-195
23. Pesek J.J., and Frost J.H. Decomposition of thiazolidines in acidic and basic solution. Spectroscopic evidence for Schiff base intermediates. Tetrahedron 31 (1975) 907-913
24. Szilágyi L., and Györgydeák Z. Comments on the putative stereoselectivity in cysteine-aldehyde reactions. Selective C(2) inversion and C(4) epimerization in thiazolidine-4-carboxylic acids. J Am Chem Soc 101 (1979) 427-432
25. Bi X., Hartono D., and Yang K.L. Controlling orientations of immobilized oligopeptides using N-terminal cysteine labels. Langmuir 24 (2008) 5238-5240
26. Zatsepin T.S., Stetsenko D.A., Arzumanov A.A., Romanova E.A., Gait M.J., and Oretskaya T.S. Synthesis of peptide-oligonucleotide conjugates with single and multiple peptides attached to 2′-aldehydes through thiazolidine, oxime, and hydrazine linkages. Bioconjug Chem 13 (2002) 822-830
27. Shao J., and Tam J.P. Unprotected peptides as building blocks for the synthesis of peptide dendrimers with oxime, hydrazone and thiazolidine linkages. J Am Chem Soc 117 (1995) 3893-3899
28. Sio C.F., and Quax W.J. Improved β-lactam acylases and their use as industrial biocatalysts. Curr Opin Biotechnol 15 (2004) 349-355
29. Arroyo M., De La Mata I., Acebal C., and Castillón M.P. Biotechnological applications of penicillin acylases: state-of-the-art. Appl Microbiol Biotechnol 60 (2003) 507-514
30. Fernández-Lafuente R., Rosell C.M., Piatkowska B., and Guisán J.M. Synthesis of antibiotics (cephaloglycin) catalyzed by penicillin G acylase: evaluation and optimization of different synthetic approaches. Enzyme Microb Technol 19 (1996) 9-14
31. Chen C.-X., Wu Q., Liu B.-K., Lv D.-S., and Lin X.-F. Anhydrous tert-pentanol as a novel media for the efficient enzymatic synthesis of amoxicillin. Enzyme Microb Technol 42 (2008) 601-607
32. Rolland-Fulcrand V., Rolland M., Roumestant M.-L., and Martinez J. Chemoenzymatic synthesis of enantiomerically pure (2S,3R,4S)-4-hydroxyisoleucine, an insulinotropic amino acid isolated from fenugreek seeds. Eur J Org Chem 4 (2004) 873-877
33. Schmidt-Dannert C., Rúa M.L., and Schmid R.D. Two novel lipases from thermophile Bacillus thermocatenulatus: screening, purification, cloning, overexpression, and properties. Methods Enzymol 284 (1997) 194-222
34. Schmidt-Dannert C., Rua M.L., Wahl S., and Schmid R.D. Bacillus thermocatenulatus lipase: a thermoalkalophilic lipase with interesting properties. Biochem Soc Trans 25 (1997) 178-182
35. Schmidt-Dannert C., Rúa M.L., Atomi H., and Schmid R.D. Thermoalkalophilic lipase of Bacillus thermocatenulatus. I. Molecular cloning, nucleotide sequence, purification and some properties. Biochim Biophys Acta, Lipids Lipid Metab 1301 (1996) 105-114
36. Schmidt-Dannert C., Sztajer H., Stocklein W., and Schmid R.D. Screening, purification and properties of a thermophilic lipase from Bacillus thermocatenulatus. Biochim Biophys Acta, Lipids Lipid Metab 1214 (1994) 43-53
37. Palomo J.M., Fernández-Lorente G., Rúa M.L., Guisán J.M., and Fernández-Lafuente R. Evaluation of the lipase from Bacillus thermocatenulatus as an enantioselective biocatalyst. Tetrahedron Asymmetry 14 (2003) 3679-3687
38. Martín J.R., Nus M., Gago J.V.S., and Sánchez-Montero J.M. Selective esterification of phthalic acids in two ionic liquids at high temperatures using a thermostable lipase of Bacillus thermocatenulatus: a comparative study. J Mol Catal B: Enzym 52-53 (2008) 162-167
39. Fechtig B., Peter H., Bickel H., and Vischer E. Concerning the preparation of 7-amino-cephalosporanic acid. Helv Chim Acta 51 (1968) 1108-1119
40. Palomo J.M., Segura R.L., Fernández-Lorente G., Pernas M., Rua M.L., Guisán J.M., et al. Purification, immobilization, and stabilization of a lipase from Bacillus thermocatenulatus by interfacial adsorption on hydrophobic supports. Biotechnol Prog 20 2 (2004) 630-635
41. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal Biochem 72 1-2 (1976) 248-254
42. López-Gallego F., Betancor L., Hidalgo A., Mateo C., Guisán J.M., and Fernández-Lafuente R. Optimization of an industrial biocatalyst of glutaryl acylase: stabilization of the enzyme by multipoint covalent attachment onto new amino-epoxy sepabeads. J Biotechnol 111 2 (2004) 219-227
43. López-Gallego F., Montes T., Fuentes M., Alonso N., Grazu V., Betancor L., et al. Improved stabilization of chemically aminated enzymes via multipoint covalent attachment on glyoxyl supports. J Biotechnol 116 (2005) 1-10
44. Rosell C.M., Fernández-Lafuente R., and Guisán J.M. Modification of enzyme properties by the use of inhibitors during their stabilization by multipoint covalent attachment. Biocatal Biotransform 12 (1995) 67-76
45. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277 (1970) 680-685
46. Kutzbach C., and Rauenbusch E. Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11105. Hoppe-Seyler's Z Physiol Chem 355 (1974) 45-53
47. Duggleby H.J., Tolley S.P., Hill G.P., Dodson E.J., Dodson G., and Moody P.C. Penicillin acylase has a single-amino-acid catalytic centre. Nature 373 (1995) 264-268
48. Carrasco-López C., Godoy C., de las Rivas B., Fernández-Lorente G., Palomo J.M., Guisán J.M., et al. Activation of bacterial thermoalkalophilic lipases is spurred by dramatic structural rearrangements. J Biol Chem 284 (2009) 4365-4372
49. Matsuda A., Matsuyama K., Yamamoto K., Ichikawa S., and Komatsu K.-I. Cloning and characterization of the genes for two distinct cephalosporin acylases from a Pseudomonas strain. J Bacteriol 169 (1987) 5815-5820
50. Aramori I., Fukagawa M., Tsumura M., Iwami M., Isogai T., Ono H., et al. Cloning and nucleotide sequencing of new glutaryl 7-ACA and cephalosporin C acylase genes from Pseudomonas strains. J Ferment Bioeng 72 (1991) 232-243
51. Fernandez-Lorente G., Godoy C., Lopez-Gallego F., Grazu V., de las Rivas B., Palomo J.M., et al. Solid-phase chemical amination of a lipase from Bacillus thermocatenulatus to improve its stabilization via covalent immobilization on highly activated glyoxyl-agarose. Biomacromolecules 9 (2008) 2553-2561
52. Girelli A.M., Mattei E., and Messina A. Immobilized tyrosinase reactor for on-line HPLC application. Development and characterization. Sens Actuator B-Chem 121 (2007) 515-521
53. Hornsey V.S., Prowse C.V., and Pepper D.S. Reductive amination for solid-phase coupling of protein. A practical alternative to cyanogen bromide. J Immunol Methods 93 (1986) 83-88
54. Weingarten S., and Thiem J. Facile formation of novel carbohydrate-amino acid conjugates by reductive amination. Synlett (2003) 1052-1054
55. Burteau N., Burton S., and Crichton R.R. Stabilisation and immobilisation of penicillin amidase. FEBS Lett 258 (1989) 185-189