Horseradish peroxidase thermostabilization: The combinatorial effects of the surface modification and the polyols

Enzyme and Microbial Technology

Volumn 38, Issue 1-2, 2006, Pages 118-125

  Hassani, Leila ^a   Ranjbar, Bijan ^a   Khajeh, Khosro ^a   Naderi Manesh, Hossein ^a   Naderi Manesh, Mehdi ^a   Sadeghi, Mehdi ^b  

^a TARBIAT MODARES UNIVERSITY   (Iran)

^b NATIONAL INSTITUTE OF GENETIC ENGINEERING AND BIOTECHNOLOGY   (Iran)

Author keywords

Chemical modification; Circular dichroism; Citraconic anhydride; Horseradish peroxidase; Polyols; Thermal stability; Thermoinactivation

Indexed keywords

BIOREMEDIATION; BIOSENSORS; BIOTECHNOLOGY; CHEMICAL MODIFICATION; DIAGNOSIS; ENZYME KINETICS; PLANTS (BOTANY); THERMODYNAMIC STABILITY;

CIRCULAR DICHROISM; HORSERADISH PEROXIDASE; POLYOLS; THERMOINACTIVATION;

ENZYMES;

CITRACONIC ANHYDRIDE; HORSERADISH PEROXIDASE; POLYOL;

ARTICLE; CHEMICAL MODIFICATION; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; ENZYME INACTIVATION; ENZYME MODIFICATION; ENZYME STABILITY; KINETICS; PROTECTION; THERMODYNAMICS; THERMOSTABILITY;

ARMORACIA RUSTICANA;

EID: 27844536480     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.05.006     Document Type: Article

References (58)

1. S. Janecek Strategies for obtaining stable enzymes Process Biochem 28 1993 435 445
2. A. Shaw, and R. Bott Engineering enzymes for stability Curr Opin Struct Biol 6 1996 540 551
3. C.O. Fagain Understanding and increasing protein stability Biochim Biophys Acta 1252 1995 1 14
4. A. Illanes Stability of biocatalysts Electron J Biotechnol 2 1999 1 12
5. C.O. Fagain Enzyme stabilization - recent experimental progress Enzyme Microb Technol 33 2003 137 149
6. H.B. Dunford Peroxidases in Chemistry and Biology 1989 CRC Press Boca Raton, FL, US
7. E. Miland, R.S. Malcolm, and C.O. Fagain Modification of horseradish peroxidase with bifunctional N-hydroxysuccinimide esters: effects on molecular stability Enzyme Microb Technol 19 1996 242 249
8. O. Ryan, M.R. Smyth, C.O. Fagain, Horseradish Peroxidase: The Analysts Friend. London: Protland Press; 1994.
9. N.C. Veitch, and A.T. Smith Horseradish peroxidase Adv Inorg Chem 51 2001 107 162
10. R. Krieg, and K.J. Halbhuber Recent advances in catalytic peroxidase histochemistry Cell Mol Biol 49 2003 547 563
11. N.C. Veitch Horseradish peroxidase: a modern view of a classic enzyme Phytochemistry 65 2004 249 259
12. K. Chattopadhyay, and S.M. Mazumdar Structural and conformational stability of horseradish peroxidase: effect of temperature and pH Biochemistry 39 2000 263 270
13. M. Gajhede, D.J. Schuller, A. Henricksen, A.T. Smith, and T.L. Poulos Crystal structure determination of classical horseradish peroxidase at 2.15 Å resolution Nat Struct Biol 4 1997 1032 1039
14. V.P. Torchilin, A.V. Maksimenko, V.N. Smirnov, I.V. Berezin, A.M. Klibanov, and K. Martinek The principles of enzyme stabilization IV modification of 'key' functional groups in the tertiary structure of proteins Biochim Biophys Acta 567 1979 1 11
15. O. Ryan, M.R. Smyth, and C.O. Fagain Thermostabilized chemical derivatives of horseradish peroxidase Enzyme Microb Technol 16 1994 501 505
16. E. Miland, M.R. Smyth, and C.O. Fagain Increased thermal and solvent tolerance of acetylated horseradish peroxidase Enzyme Microb Technol 19 1996 63 67
17. E. Miland, M.R. Smyth, and C.O. Fagain Modification of horseradish peroxidase with bifunctional N-hydroxysuccinimide esters: effects on molecular stability Enzyme Microb Technol 19 1996 242 249
18. V.V. Mozhaev, V.A. Aiksnis, N.S. Melik-Nubarov, N.Z. Galkantaite, G.J. Denis, and E.P. Butkus Protein stabilization via hydrophilization: Covalent modification of trypsin and α-chymotrypsin Eur J Biochem 173 1998 147 154
19. V.V. Mozhaev, N.S. Melik-Nubarov, V.Y. Levitsky, V.A. Siksins, and K. Martinek High stability to irreversible inactivation at elevated temperatures of enzymes covalently modified by hydrophilic reagents: α-chymotrypsin Biotechnol Bioeng 40 1992 650 662
20. S. Hosseinkhani, B. Ranjbar, H. Naderi-Manesh, and M. Nemat-Gorgani Chemical modification of glucose oxidase: Possible formation of molten globule-like intermediate structure FEBS Lett. 561 2004 213 216
21. V.V. Mozhaev, I.V. Berezin, and K. Martinek Structure-stability relationship in proteins: fundamental tasks and strategy for the development of stabilized enzyme catalysts for biotechnology CRC Crit Rev Biochem Mol Biol 23 1988 235 281
22. S.S. Wong, and L.J.C. Wong Chemical cross-linking and the stabilization of proteins and enzymes Enzyme Microb Technol 14 1992 866 874
23. K. Khajeh, H. Naderi-Manesh, B. Ranjbar, A.A. Moosavi-Movahedi, and M. Nemat-Gorgani Chemical modification of lysine residues in Bacillus α-amylases: effect on activity and stability Enzyme Microb Technol 28 2001 543 549
24. K. Khajeh, B. Ranjbar, H. Naderi-Manesh, A. Ebrahim Habibi, and M. Nemat-Gorgani Chemical modification of bacterial α-amylases: changes in tertiary structures and the effect of additional calcium Biochim Biophys Acta 36467 2001 1 9
25. Y. Qu, C.L. Bolen, and D.W. Bolen Osmolyte-driven contraction of a random coil protein Proc Natl Acad Sci USA 95 1998 9268 9273
26. J.K. Kaushik, and R. Bhat Thermal stability of proteins in aqueous polyol solutions J Phys Chem 102 1998 7058 7066
27. F. Anjum, V. Rishi, and F. Ahmad Compatibility of osmolytes with Gibbs energy of stabilization of proteins Biochim Biophys Acta 1476 2000 75 84
28. M. Miroliaei, and M. Nemat-Gorgani Sugars protect native and apo yeast alcohol dehydrogenase against irreversible thermoinactivation Enzyme Microb Technol 29 2001 54 559
29. N.N. Ugarova, G.D. Rozhkova, and I.V. Berezin Chemical modification of the ε-amino groups of lysine residues in horseradish peroxidase and its effect on the catalytic properties and thermostability of the enzyme Biochim Biophys Acta 570 1979 31 42
30. D.G. Pina, A.V. Shnyrova, F. Gavilanes, A. Rodriguez, F. Leal, and M.G. Roig Thermally induced conformational changes in horseradish peroxidase Eur J Biochem 268 2001 120 126
31. 1H-NMR studies of horseradish peroxidase C and its interaction with indole-3-propionic acid Eur J Biochem 189 1990 351 362
32. P. Trinder Determination of glucose in blood using glucose oxidase with an alternative oxygen acceptor Ann Clin Biochem 6 1966 24 27
33. L.M. Shanon, E. Kay, and J.Y. Lew Peroxidase isoenzymes from horseradish roots: Isolation and physical properties J Biol Chem 241 1966 2166
34. H.B.F. Dixon, and R.N. Perham Reversible blocking of amino groups with citraconic anhydride Biochem J 109 1968 312 313
35. R. Fields The measurement of amino groups in proteins and peptides Biochem J 124 1971 581 590
36. R. Fraczkiewicz, and W. Braun Exact and efficient analytical calculation of the accessible surface areas and their gradients for macromolecules J Comp Chem 19 1998 319 333
37. A. Guagliardi, L. Cerchia, and M. Rossi Prevention of in vitro protein thermal aggregation by the solfolobus solataricus chaperonin J Biol Chem 270 1995 28126 28132
38. D.B. Wetlaufer, and Y. Xie Control of aggregation in protein refolding: a variety of surfactants promote renaturation of carbonic anhydrase II Protein Sci 4 1995 1535 1543
39. H. Paulikova, M. Molanarova, and D. Podhradsky The effect of heparin and pentosan polysulfate on the thermal stability of yeast alcohol dehydragenase Biochem Mol Biol Int 46 1998 887 894
40. Y.L. Zhang, J.M. Zhou, and C.L. Ysou Inactivation preceedes conformation change during thermal denaturation of adenylate kinase Biochim Biophys Acta 1164 1993 61 67
41. S. Zale, and A.M. Klibanov Why dose ribonuclease irreversibly inactivate at high temperatures Biochemistry 25 1986 5432 5444
42. P.H. Schippers, and H.P.J.M. Dekkers Direct determination of absolute circular dichroism data and calibration of commertial instrument Anal Chem 53 1981 778 788
43. T. Takakuwa, T. Konno, and H. Meguro A new standard substance for calibration of circular dichroism: Ammonium d-10-camphorsulfonate Anal Sci 1 1985 215 225
44. I. Protasevich, B. Ranjbar, V. Lobachov, A. Makarov, R. Gilli, and C. Briand Conformation and thermal denaturation of apocalmodulin: role of electrostatic mutations Biochemistry 36 1997 2017 2024
45. A. Christian, and A. Belarbi Kinetics of thermal deactivation of the enzymes: a simple three parameters phenomenological model can describe the decay of ezyme activity, irrespectively of mechanism Enzyme Microb Technol 27 2000 612 618
46. A.M. O'Brien, C.O. Fagain, P.F. Nielsen, and K.G. Welinder Location of crosslinks in chemically stabilized horseradish peroxidase: implications for design of crosslinks Biotechnol Bioeng 76 2001 277 284
47. R. Lumry, and H. Eyring Conformational changes of proteins J Phys Chem 58 1954 110 120
48. E.M. Strickland Circular dichroism of horseradish peroxidase and its enzyme-substrate compounds Biochim Biophys Acta 151 1968 70 75
49. M. Akita, D. Tsutsumi, M. Kobayashi, and H. Kise Structural change and catalytic activity of Horseradish peroxidase in oxidative polymerization of phenol Biosci Biotechnol Biochem 65 2001 1581 1588
50. A. Schmidt, J. Schumacher, J. Reichelt, H. Hecht, and U. Bilitewski Mechanistic and molecular investigations on stabilization of Horseradish peroxidase C Anal Chem 74 2002 3037 3045
51. S.M. Kelly, and N.C. Price Application of circular dichroism to studies of protein folding and unfolding Biochim Biophys Acta 1338 1997 161 185
52. K. Welinder Amino acid sequence studies of horseradish peroxidase Eur J Biochem 96 1979 483 502
53. P.J.G. Butter, and B.S. Hartley Methods in Enzymology vol. 25B 1973 Academic Press New York p. 191-199
54. V.V. Mozhaev Mechanism-based strategies for protein thermostabilization Tibtech 11 1993 88 95
55. J. Fitter, R. Herrmann, N.A. Dencher, A. Blume, and T. Hauss Activity and stability of thermostable α-amylase compared to its mesophilic homologue: Mechanism of thermal adaptation Biochemistry 40 2001 10723 10731
56. K.A. Dill Dominant forces in protein folding Biochemistry 29 1990 7133 7155
57. S.N. Timasheff Water as ligand: preferential binding and exclusion of denaturants in protein unfolding Biochemistry 31 1992 7 9864
58. S. Matsue, F. Tomoyuki, and O. Miyawaki Effects of water activity and aqueous solvent ordering on thermal stability of lysozyme, α- chymotrypsinogen A, and alcohol dehydrogenase Int J Biol Macromol 28 2001 343 349