Chemical modification results in hyperactivation and thermostabilization of Fusarium solani glucoamylase

Canadian Journal of Microbiology

Volumn 53, Issue 2, 2007, Pages 177-185

  Bhatti, Haq Nawaz ^a   Rashid, M Hamid ^b   Asgher, Muhammad ^a   Nawaz, Rakhshanda ^a   Khalid, A M ^b   Perveen, Raheela ^b  

^a UNIVERSITY OF AGRICULTURE   (Pakistan)

^b NATIONAL INSTITUTE FOR BIOTECHNOLOGY AND GENETIC ENGINEERING NIBGE   (Pakistan)

Author keywords

Carboxylic group modification; Fusarium solani; Glucoamylase; Hydophobization; Thermostability

Indexed keywords

CHYMOTRYPSIN; ETHYLENEDIAMINE; FUSARIUM SOLANI; GLUCOAMYLASE; HYDOPHOBIZATION; THERMAL DENATURATION; THERMAL UNFOLDING;

CATALYST ACTIVITY; CHEMICAL MODIFICATION; FREE ENERGY; FUNGI; HYDROLYSIS; NUCLEOPHILES; THERMODYNAMIC STABILITY;

ENZYME KINETICS;

1 ETHYL 3(3 DIMETHYLAMINOPROPYL)CARBODIIMIDE; CHYMOTRYPSIN A; ETHYLENEDIAMINE; FUNGAL ENZYME; GLUCAN 1,4 ALPHA GLUCOSIDASE; IMIDE; SUBTILISIN; UNCLASSIFIED DRUG;

CARBOXYLIC ACID; ETHYLENE; FUNGUS; GLUCOSE; HYDROPHOBICITY; PATHOGEN;

ARTICLE; CHEMICAL MODIFICATION; ENZYME ACTIVATION; ENZYME MECHANISM; FUSARIUM SOLANI; NONHUMAN; PRIORITY JOURNAL; TEMPERATURE DEPENDENCE; THERMOSTABILITY;

BINDING SITES; ENZYME ACTIVATION; ENZYME STABILITY; FUSARIUM; GLUCAN 1,4-ALPHA-GLUCOSIDASE; HYDROGEN-ION CONCENTRATION; TEMPERATURE; THERMODYNAMICS;

FUNGI; FUSARIUM SOLANI;

EID: 34249735343     PISSN: 00084166     EISSN: None     Source Type: Journal    
DOI: 10.1139/W06-094     Document Type: Article

References (32)

1. Afzal, A.J., Bokhari, S.A., Ahmad, W., Rashid, M.H., Rajoka, M.I., and Siddiqui, K.S. 2000. Two simple and rapid methods for the detection of polymer degrading enzymes on high resolution alkaline cold in situ native (HiRACIN-PAGE) and high resolution in situ inhibited native (HiRACIN-PAGE). Biotechnol. Lett. 46: 11-16.
2. Bhatti, H.N., Rashid, M.H., Nawaz, R., Perveen, R., Jabbar, A., and Asgher, M. 2007. Purification and characterization of a novel glucoamylase from Fusarium solani. Food Chem. 103 : 338-343.
3. Bourne, Y., and Henrissat, B. 2001. Glycoside hydrolases and glycosyltransferases: families and functional modules. Curr. Opin. Struct. Biol. 11: 593-600. doi:10.1016/S0959-440X(00)00253-0.
4. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
5. Eyring, H., and Stearn, A.E. 1924. The application of the theory of absolute reaction rates to protein. Chem. Rev. 24: 253-270.
6. Fagain, C.O., and Kennedy, R. 1991. Functionally stabilized proteins - a review. Biotechnol. Adv. 9: 351-405.
7. Fogarty, W.M. 1983. Microbial amylases. In Microbial enzyme and biotechnology. Edited by W.M Fogarty. Applied Science Publishers, London, U.K. pp. 1-90.
8. Georis, J., Esteves, F.L., Brasseur, J.L., Bougnet, V., Devreese, B., Giannotta, F., Granier, B., and Frere, J.M. 2000. An additional aromatic interaction improves the thermostability and thermophilicity of a mesophilic family 11 xylanase: structural basis and molecular study. Protein Sci. 9: 466-475.
9. Hamid Rashid, M.H., Najmus-Saqib, A.A., Rajoka, M.I., and Siddiqui, K.S. 1997. Native enzyme mobility shift assay (NEMSA): a new method for monitoring the carboxyl group modification of CMCase from Aspergillus niger. Biotechnol. Tech. 11: 245-247. doi:10.1023/A:1018486404960.
10. Imoto, T. 1997. Stabilization of proteins. Cell. Mol. Life Sci. 53: 215-223. doi:10.1007/PL00000593.
11. Iqbal, Z., Rashid, M.H., Jabbar, A., Malana, M.A., Khalid, A.M., and Rajoka, M.I. 2003. Kinetics of enhanced thermostability of an extracellular glucoamylase from Arachniotus sp. Biotechnol. Lett. 25: 1667-1670. doi:10.1023/A:1025665831426.
12. Jaenicke, R. 1991. Protein stability and molecular adaptation to extreme conditions. Eur. J. Biochem. 202: 715-728. doi:10.1111/j.1432-1033.1991. tb16426.x.
13. Khajeh, K., Manesh, H.N., Ranjbar, B., Movahedi, A.M., and Gorgani, M.V. 2001. Chemical modification of lysine residues in Bacillus α-amylases: effect on activity and stability. Enzyme Microb. Technol. 28: 543-549. doi:10.1016/S0141-0229(01)00296-4.
14. Khan, M.A.K., Reilly, P.J., and Ford, C. 2000. Thermal and molecular characterization of Aspergillus awamori glucoamylase catalytic and starch binding domains. Starch Staerke, 52: 358-397.
15. Miland, E., Smyth, M.R., and Fagain, C.O. 1996. Increased thermal and solvent tolerance of acetylated horseradish peroxidase. Enzyme Microb. Technol. 19: 63-67. doi:10.1016/0141-0229(95)00169-7.
16. Montes, F.J., Battanar, E., Catalan, J., and Galan, M.A. 1995. Kinetics and heat inactivation mechanism of D-amino oxidase. Process Biochem. 30: 217-224. doi:10.1016/0032-9592(95)95720-4.
17. Mozhaev, V.V., Melik-Nubarov, N.S., Levitsky, V.Y., Siksirs, V.A., and Martinek, K. 1992. High stability to irreversible inactivation at elevated temperatures of enzymes covalently modified by hydrophilic reagents: α-chymotrypsin. Biotechnol. Bioeng. 40: 650-662. doi:10.1002/bit.260400603.
18. Munch, O., and Tritsch, D. 1990. Irreversible thermo-inactivation of glycoamylase from Aspergillus niger and thermostabilization by chemical modification of carboxyl groups. Biochim. Biophys. Acta, 1041: 111-116.
19. Niaz, M., Ghafoor, M.Y., Jabbar, A., Wahid, A., Rasul, E., Ahmed, R., and Rashid, M.H. 2004. Properties of glucoamylase from a mesophilic fungus Arachniotus citrinus produced under solid-state growth condition. Int. J. Biol. Biotechnol. 1: 223-231.
20. Rashid, M.H., and Siddiqui, K.S. 1998. Thermodynamic and kinetic study of stability of the native and chemically modified β-glucosidase from Aspergillus niger. Process Biochem. 33: 109-115. doi:10.1016/S0032-9592(97)00036-8.
21. Reilly, P.J., and Ames, I.A. 1999. Protein engineering of glucoamylase to improve industrial performance - a review. Starch Staerke, 51: 269-274.
22. Savel'ev, A.N., and Firsov, L.M. 1983. Effect of modifications of a series of amino acid radicals on the enzymatic activity of glucoamylase from Aspergillus awamori. Biokhimiia, 48: 1311-1318.
23. Selvakumar, P., Ashakumary, L., Helen, A., and Pandey, A. 1996. Purification and characterization of glucoamylase produced by Aspergillus niger in solid state fermentation. Lett. Appl. Microbiol. 23: 403-406.
24. Semimaru, T., Goto, M., Furudawa, K., and Hayashida, K. 1995. Functional analysis of the threonine and serine-rich Gp-1 domain of glucoamylase 1 from A. awamori var kawachi. Appl. Environ. Microbiol. 61: 2885-2890.
25. Siddiqui, K.S., Azhar, M.J., Rashid, M.H., and Rajoka, M.I. 1997. Stability and identification of active site residues of carboxymethylcellulase from Aspergillus niger and Cellulomonas biazotea. Folia Microbiol. (Praha), 42: 312-318.
26. Siddiqui, K.S., Shemsi, A.M., Anwar, M.A., Rashid, M.H., and Rajoka, M.I. 1999. Partial and complete alteration of surface charges of carboxymethylcellulase by chemical modification: thermostabilization in water-miscible organic solvent. Enzyme Microb. Technol. 24: 599-608. doi:10.1016/S0141-0229(98)00170-7.
27. Siddiqui, K.S., Saqib, A.N., Rashid, M.H., and Rajoka, M.I. 2000. Carboxyl group modification significantly altered the kinetic properties of purified carboxymethylcellulase from Aspergillus niger. Enzyme Microb. Technol. 27: 467-474. doi:10.1016/S0141-0229(00)00254-4.
28. Torchilin, V.P., Maksimenko, A.V., Smirnov, V.N., Berezin, I.V., and Martinek, K. 1979. The principles of enzyme stabilization. IV. 'Key' functional groups in tertiary structure of proteins and the effect of their modifications on thermostability of enzymes. Biochim. Biophys. Acta, 567: 1-11.
29. Tripton, K.F., and Dixon, H.B.F.1979. Effects of pH on enzymes. Methods Enzymol. 63: 183-234. doi:10.1016/0076-6879(79)63011-2.
30. Vieille, C., and Zeikus, J.G. 1996. Thermozymes: identifying molecular determinants of protein structural and functional stability. Trends Biotechnol. 14: 183-190. doi:10.1016/0167-7799(96)10026-3.
31. Violet, M., and Munier, J.C. 1989. Kinetic study of irreversible thermal denaturation of Bacillus licheniformis α-amylase. Biochem. J. 163: 665-670.
32. Wong, S.S., and Wong, L.J.C. 1992. Chemical cross-linking and the stabilization of proteins and enzymes. Enzyme Microb. Technol. 14: 866-874. doi:10.1016/0141-0229(92)90049-T.