Discrimination among eight modified Michaelis-Menten kinetics models of cellulose hydrolysis with a large range of substrate/enzyme ratios: Inhibition by cellobiose

Applied Biochemistry and Biotechnology - Part A Enzyme Engineering and Biotechnology

Volumn 112, Issue 3, 2004, Pages 173-184

  Bezerra, Rui M F ^a   Dias, Albino A ^a  

^a UNIVERSITY OF TRÁS OS MONTES AND ALTO DOURO   (Portugal)

Author keywords

Cellobiose inhibition; Cellulase kinetics; Enzyme substrate complex; Exoglucanase Cel7A; Integrated Michaelis Menten equations; Trichoderma reesei

Indexed keywords

CATALYSIS; CELLULOSE; HYDROLYSIS; LEAST SQUARES APPROXIMATIONS; MATHEMATICAL MODELS; PARAMETER ESTIMATION;

CELLULOSE HYDROLYSIS; MICHAELIS-MENTEN KINETICS MODELS; PARABOLIC INHIBITION; TRICHODERMA REESEI;

ENZYME KINETICS;

BETA GLUCOSIDASE; CELLOBIOSE; CELLULASE; CELLULOSE; EXOGLUCANASE; UNCLASSIFIED DRUG; 4 NITROPHENYL BETA D GLUCOSIDE; 4-NITROPHENYL BETA-D-GLUCOSIDE; CARBOXYMETHYLCELLULOSE; CELLULOSE 1,4 BETA CELLOBIOSIDASE; ENZYME INHIBITOR; GLUCOSIDE;

AFFINITY CHROMATOGRAPHY; ARTICLE; CATALYSIS; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME INHIBITION; ENZYME INHIBITOR COMPLEX; ENZYME PURIFICATION; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; GEL FILTRATION CHROMATOGRAPHY; HYDROLYSIS; INHIBITION KINETICS; MICHAELIS MENTEN KINETICS; NONHUMAN; TRICHODERMA REESEI; ULTRAFILTRATION; ALGORITHM; CHEMICAL MODEL; CHEMISTRY; COMPUTER SIMULATION; ENZYME STABILITY; ENZYMOLOGY; KINETICS; METABOLISM; REGRESSION ANALYSIS; TRICHODERMA;

CATALYSTS; CELLOBIOSE; CELLULOSE; ENZYMATIC ACTIVITY; HYDROLYSIS; MATHEMATICAL MODELS;

HYPOCREA JECORINA; TRICHODERMA;

ALGORITHMS; CARBOXYMETHYLCELLULOSE; CELLOBIOSE; CELLULOSE; CELLULOSE 1,4-BETA-CELLOBIOSIDASE; COMPUTER SIMULATION; ENZYME INHIBITORS; ENZYME STABILITY; GLUCOSIDES; HYDROLYSIS; KINETICS; LEAST-SQUARES ANALYSIS; MODELS, CHEMICAL; TRICHODERMA;

EID: 3042698636     PISSN: 02732289     EISSN: None     Source Type: Journal    
DOI: 10.1385/ABAB:112:3:173     Document Type: Article

References (41)

1. Ladisch, M. R. and Svarczkopf, J. A. (1991), Bioresour. Technol. 36, 83-95.
2. Kurakake, M., Shirasawa, T., Ooshima, H., Converse, A. O., and Kato, J. (1995), Appl. Biochem. Biotechnol. 50, 231-241.
3. Howell, J. A. and Mangat, M. (1978), Biotechnol. Bioeng. 20, 847-863.
4. Nidetzky, B., Steiner, W., Hayn, M., and Esterbauer, H. (1993), Bioresour. Technol. 44, 25-32.
5. Lee, Y.-H. and Fan, L. T. (1982), Biotechnol. Bioeng. 24, 2383-2406.
6. Pereira, A. N. (1987), PhD thesis, Purdue University, West Lafayette, IN.
7. Kim, D. W., Kim, T. S., Jeong, Y. K., and Lee, J. K. (1992), J. Ferment. Bioeng. 73(6), 461-466.
8. Nidetzky, B., Hayn, M., Macarron, R., and Steiner, W. (1993), Biotechnol. Lett. 15(1), 71-76.
9. Eriksson, T., Karlsson, J., and Tjerneld, F. A. (2002), Appl. Biochem. Biotechnol. 101, 41-60.
10. Howell, J. A. and Stuck, J. D. (1975), Biotechnol. Bioeng. 17, 873-893.
11. Bader, J., Bellgardt, K.-H., Singh, A., Kumar, P. K. R., and Schügerl, K. (1992), Bioprocess Eng. 7, 235-240.
12. Maglione, G., Russel, J. B., and Wilson, D. B. (1997), Appl. Environ. Microbiol. 63(2), 665-669.
13. Schülein, M. J. (1997), Biotechnology 57(1-3), 71-81.
14. Bezerra, R. M. (1995), PhD thesis, Universidade de Trás-os-Montes e Alto Douro, Vila Real, Portugal.
15. Hsu, T.-A. (1979), PhD thesis, Purdue University, West Lafayette, IN.
16. Lee, Y.-H. and Fan, L. T. (1983), Biotechnol. Bioeng. 25, 939-966.
17. Beldman, G., Leeuwen, S.-V., Rombouts, F. M., and Voragen, F. G. J. (1985), Biochem. J. 146, 301-308.
18. Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. (1951), J. Biol. Chem. 193, 265-275.
19. Wood, T. M. and Bhat, K. M. (1988), Methods Enzymol 160, 87-113.
20. Klyosov, A. A. and Rabinovitch, M. L. (1980), in Enzyme Engineering Future Directions, Wingard, L. B. Jr., Berezine, I. V., and Klyosov, A. A., eds., Plenum, New York, pp. 83-165.
21. Nidetzky, B., Steiner, W., and Claeyssens, M. (1994), Biochem. J. 303, 817-823.
22. Väljamäe, P., Petterson, G., and Johansson, G. (2001), Eur. J. Biochem. 268, 4520-4526.
23. Harjunpää, V., Teleman, A., Koivula, A., Ruohonen, L., Teeri, T. T., Teleman, O., and Drakenberg, T. (1998), Eur. J. Biochem. 240, 584-591.
24. Segel, H. I. (1993), in Enzyme Kinetics, John Wiley & Sons, New York, pp. 18-89.
25. Fujii, M., Homma, T., Ooshima, K., and Taniguchi, M. (1991), Appl. Biochem. Biotechnol. 28/29, 145-156.
26. Fernly, H. N. (1974), Eur. Biochem. J. 43, 377, 378.
27. Yun, S.-L. and Suelter, C. H. (1977), Biochim. Biophys. Acta 480, 1-13.
28. Mangat, M. N. and Howell, J. A. (1978), Food Pharm. Bioeng. 74(172), 77-81.
29. Ladisch, M. R., Lin, K. W., Voloch, M., and Tsao, G. T. (1983), Enzyme Microb. Technol. 5(2), 81-102.
30. Chose, T. K., Roychoudhury, P. K., and Ghosh, P. (1984), Biotechnol. Bioeng. 26, 377-381.
31. Golovchenko, N. P., Kataeva, I. A., and Akimenko, V. K. (1992), Enzyme Microb. Technol. 14, 327-331.
32. Orgeret, C., Seillier, E., Gautier, C., Defaye, J., and Driguez, H. (1992), Carbohydr. Res. 224, 29-40.
33. Lee, Y.-H. and Fan, L. T. (1983), Biotechnol. Bioeng. 25, 939-966.
34. Holtzapple, M., Cognata, M., Shu, Y., and Hendrickson, C. (1990), Biotechnol. Bioeng. 36, 275-287.
35. Duggleby, R. G. (1995), Methods Enzymol. 249, 61-90.
36. Selwyn, M. J. (1965), Biochim. Biophys. Acta 105, 193-195.
37. Ralston, M. L. and Jennrich, R. I. (1978), Technometrics 20(1), 7-14.
38. Mannervik, B. (1982), Methods Enzymol. 87C, 370-391.
39. Igarashi, K., Samejima, M., and Eriksson K.-E. L. (1998), Eur. J. Biochem. 253, 101-106.
40. Henriksson, H., Ståhlberg, J., Isaksson, R., and Pettersson, G. (1996), FEBS Lett. 390, 339-344.
41. Ladisch, M. R., Hong, J., Voloch, M., and Tsao, G. T. (1981), in Trends in the Biology of Fermentations for Fuels and Chemicals, Hollaender, A., Rabson, R., Pietro, R., and Wolfe, eds., Plenum, New York, pp. 55-83.