Thermalstabilization of chitinolytic enzymes of Pantoea dispersa

Biochemical Engineering Journal

Volumn 35, Issue 2, 2007, Pages 150-157

  Gohel, V ^a,b   Naseby, D C ^a  

^a UNIVERSITY OF HERTFORDSHIRE   (United Kingdom)

^b Faculty of Science   (India)

Author keywords

Chitinase; Pantoea dispersa; pH; Salts; Stability; Temperature; Thermodynamic

Indexed keywords

BIOCONTROL AGENT; CHITINASE; DEACTIVATION KINETICS; PANTOEA DISPERSA;

ACTIVATION ENERGY; BIOCONTROL; SODIUM CHLORIDE; THERMODYNAMIC STABILITY;

ENZYMES;

BACTERIAL ENZYME; CHITINASE; CHITINASE I; CHITINASE II; CHITINASE III; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ARTICLE; ENERGY; ENTHALPY; ENTROPY; ISOLATION PROCEDURE; NONHUMAN; PANTOEA; PH MEASUREMENT; PRIORITY JOURNAL; THERMODYNAMICS; THERMOSTABILITY;

HYPOCREA LIXII; PANTOEA DISPERSA;

EID: 34247857485     PISSN: 1369703X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bej.2007.01.009     Document Type: Article

References (46)

1. Sándor E., Pusztahelyi T., Karaffa L., Karányi Z., Pócsi I., Sándor B., Szentirmai A., and Pócsi I. Allosamidin inhibits the fragmentation of Acremonium chrysogenum but does not influence the cephalosporin-C production of the fungus. FEMS Microbiol. Lett. 164 (1998) 231-236
2. van Aalten D.M.F., Komander D., Synstad B., Gaseidnes S., Peter M.G., and Eijsink V.G.H. Structural insights into the catalytic mechanism of a family 18 exo-chitinase. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 8979-8984
3. Watanabe T., Oyanagi W., Suzuki K., and Tanaka H. Chitinase system of Bacillus circulans WL-12 and importance of chitinase A1 in chitin degradation. J. Bacteriol. 172 (1990) 4017-4022
4. Sakai K., Yokota A., Kurokawa H., Wakayama M., and Moriguchi M. Purification and characterization of three thermostable endochitinases of a noble Bacillus strain, MH-1, isolated from chitin-containing compost. Appl. Environ. Microbiol. 64 (1998) 3397-3402
5. Mavromatis K., Lorito M., Woo S.L., and Bouriotis V. Mode of action and antifungal properties of two cold-adapted chitinases. Extremophiles 7 (2003) 385-390
6. Deshpande M.V. Enzymatic degradation of chitin and its biological applications. J. Sci. Ind. Res. 45 (1986) 273-281
7. Fukamizo T. Chitinolytic enzymes catalysis, substrate binding, and their application. Curr. Protein Pept. Sci. 1 (2000) 105-124
8. Boot R.G., van Achterberg T.A., van Aken B.E., Renkema G.H., Jacobs M.J., Aerts J.M., and de Vries C.J. Strong induction of members of the chitinase family of proteins in atherosclerosis: chitotriosidase and human cartilage gp-39 expressed in lesion macrophages. Arterioscler. Thromb. Vasc. Biol. 19 (1999) 687-694
9. Cintin C., Johasen J.S., Christensen I.J., Price P.A., Sorensen S., and Nielsen H.J. Serum YKL-40 and colorectal cancer. Br. J. Cancer 79 (1999) 1494-1499
10. Hollak C.E., van Weely S., van Oers M.H., and Aerts J.M. Marked elevation of plasma chitotriosidase activity. A novel hallmark of Gaucher disease. J. Clin. Invest. 93 (1994) 1288-1292
11. Cottaz S., Brasme B., and Driguez H. A fluorescence-quenched chitopentaose for the study of endo-chitinases and chitobiosidases. Eur. J. Biochem. 267 (2000) 5593-5600
12. Gohel V., Singh A., Maisuria V., Phadnis A., and Chhatpar H.S. Biopro spec ting and antifungal potential of chitinolytic microorganisms. Afr. J. Biotechnol. 5 (2006) 54-72
13. Jung W.J., Kuk J.H., Kim K.Y., Kim T.H., and Park R.D. Purification and characterization of chitinase from Paenibacillus illinoisensis KJA-424. J. Microbiol. Biotechnol. 15 (2005) 274-280
14. Punja Z.K., and Zhang Y.Y. Plant chitinases and their roles in resistance to fungal diseases. J. Nematol. 25 (1993) 526-540
15. Vaidya R., Vyas P., and Chhatpar H.S. Statistical optimization of medium components for the production of chitinase by Alcaligenes xylosoxydans. Enzyme Microb. Technol. 33 (2003) 92-96
16. V. Gohel, 2006. Studies on chitinase based biocontrol of pigeonpea wilt by Pantoea dispersa. PhD Thesis. Vadodara, Gujarat, India: M.S. University of Baroda.
17. Gohel V., Chaudhary T., Vyas P., and Chhatpar H.S. Statistical screening of medium components for the production of chitinase by the marine isolate Pantoea dispersa. Biochem. Eng. J. 28 (2006) 50-56
18. Vieille C., and Zeikus G.J. Hyperthermophilic enzymes: sources, uses, and molecular mechanisms for thermostability. Microbiol. Mol. Biol. Rev. 65 (2001) 1-43
19. Gåseidnes S., Synstad B., Jia X., Kjellesvik H., Vriend G., and Eijsink V.G.H. Stabilization of a chitinase from Serratia marcescens by Gly → Ala and Xxx → Pro mutations. Protein Eng. 16 (2003) 841-846
20. Mansfeld J., Vriend G., Dijkstra B.W., Veltman O.R., Van den Burg B., Venema G., Ulbrich-Hofmann R., and Eijsink V.G.H. Extreme stabilization of a thermolysin-like protease by an engineered disulfide bond. J. Biol. Chem. 272 (1997) 11152-11156
21. Rashid M.H., and Siddiqui K.S. Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidases from Aspergillus niger. Proc. Biochem. 33 (1998) 109-115
22. Blaber M., Zhang X.J., and Matthews B.W. Structural basis of amino acid alpha helix propensity. Science 260 (1993) 1637-1640
23. Chen J.P., and Chang K.C. Immobilization of chitinase on a reversibly soluble-insoluble polymer for chitin hydrolysis. J. Chem. Technol. Biotechnol. 60 (1994) 133-140
24. Matthews B.W., Nicholson H., and Becktel W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U.S.A. 84 (1987) 6663-6667
25. Kapat A., and Panda T. pH and thermal stability studies of chitinase from Trichoderma harzianum: a thermodynamic consideration. Bioprocess. Biosyst. Eng. 16 (1997) 269-272
26. Srinivas R., and Panda T. Enhancing the feasibility of many biotechnological processes through enzyme deactivation studies. Bioprocess. Eng. 21 (1999) 363-369
27. Gohel V., Chaudhary T., Vyas P., and Chhatpar H.S. Isolation and identification of marine chitinolytic bacteria and their potential in antifungal biocontrol. Indian J. Exp. Biol. 42 (2004) 715-720
28. Monreal J., and Reese E.T. The chitinase of Serratia marcescens. Can. J. Microbiol. 15 (1969) 689-696
29. Hackman R.H. Studies on chitin V: the action of mineral acids on chitin. Aust. J. Biol. Sci. 15 (1962) 526-537
30. Gohel V., Trivedi S., Vyas P., and Chhatpar H.S. Formulation of medium constituents by multiresponse analysis of central composite design to enhance chitinase production in Pantoea dispersa. Indian J. Exp. Biol. 42 (2004) 1123-1131
31. Vyas P., and Deshpande M.V. Chitinase production by Myrothecium verrucaria and its significance for fungal mycelia degradation. J. Gen. Appl. Microbiol. 35 (1989) 343-350
32. Nelson N. A photometric adaptation of the Somogyii method for the determination of glucose. J. Biol. Chem. 153 (1994) 375-380
33. Eyring H., and Stearn A.E. The application of the theory of absolute reaction rates to proteins. Chem. Rev. 24 (1939) 253-270
34. Laidler K.J., and Peterman B.F. Temperature effects in enzyme kinetics. Methods Enzymol. 63 (1979) 234-257
35. Francisco J.G.M., Maria C.A.O., and Angel M.R. Further thermal characterization of an aspartate aminotransferase from a halophilic organism. Biochem. J. 298 (1994) 465-470
36. Milan P., and Peter V. Analysis of the mechanism and kinetics of thermal inactivation of enzymes: critical assessment of isothermal inactivation experiments. Proc. Biochem. 31 (1996) 787-800
37. Lee T.S.-B., Inouye K., and Tonomura B. The states of tyrosyl residues in thermolysin as examined by nitration and pH-dependent ionization. J. Biochem. 121 (1997) 231-237
38. Arakawa T., and Tokunaga M. Electrostatic and hydrophobic interactions play a major role in the stability and refolding of halophilic proteins. Protein Pept. Lett. 11 (2004) 125-132
39. Kuniyo I., Keiko K., and Tonomura B. Sodium chloride enhances markedly the thermal stability of thermolysin as well as its catalytic activity. Biochim. Biophys. Acta 1388 (1998) 209-214
40. Zaccai G., and Eisenberg H. Halophilic proteins and the influence of solvent on protein stabilization. Trends Biochem. Sci. 15 (1990) 333-337
41. Eisenberg H., Mevarech M., and Zaccai G. Biochemical, structural, and molecular genetic aspects of halophilism. Adv. Protein Chem. 43 (1992) 1-62
42. D'Amico S., Marx J.-C., Gerday C., and Feller G. Activity-stability relationships in extremophilic enzymes. J. Biol. Chem. 278 (2003) 7891-7896
43. Voordouw G., Milo C., and Roche R.S. Further thermal characterization of an aspartate aminotransferase from a halophilic organism. Biochemistry 15 (1976) 3716-3723
44. Foster R.L. Modification of enzyme activity. In: Baron P.J. (Ed). The Nature of Enzymology (1980), Croom Helm, London 91-161
45. Declerck N., Machius M., Joyet P., Wiegand G., Huber R., and Gaillardin C. Hyperthermostabilization of Bacillus licheniformis α-amylase and modulation of its stability over a 50 °C temperature range. Protein Eng. 16 (2003) 287-293
46. Matsumura M., Signor G., and Matthews B.W. Substantial increase of protein stability by multiple disulfide bonds. Nature 342 (1989) 291-293