Corn Gluten Hydrolysis by Alcalase: Effects of Process Parameters on Hydrolysis, Solubilization and Enzyme Inactivation

D. KILIÇ APAR and B. ÖZBEK, Corn Gluten Hydrolysis by Alcalase: Effects of …, Chem. Biochem. Eng. Q. 22 (2) 203–212 (2008)

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Corn Gluten Hydrolysis by Alcalase:
Effects of Process Parameters on Hydrolysis, Solubilization and Enzyme Inactivation
D. Krlrç Apar and B. Özbek*
Yrldrz Technical University, Department of Chemical Engineering,
Davutpaºa Campus, 34210, Esenler/Istanbul, Turkey

Original scientific paper
Received: April 11, 2007
Accepted: May 31, 2007

The aim of this study was to investigate the influences of substrate concentration, enzyme concentration, temperature and pH on hydrolysis and solubilization of corn gluten as well as enzyme stability. The corn gluten was hydrolyzed by Alcalase enzyme (a bacterial protease produced by a selected strain of Bacillus licheniformis) that was chosen among five commercial enzymes examined. The optimum process conditions for hydrolysis and solubilization were obtained as 30 g L–1 substrate mass concentration, 2.5 mL L–1 enzyme concentration, 55 °C and pH 8. Under these conditions, the values of degree of hydrolysis and solubilization were found as 28.4 % and 85.3 % respectively; and enzyme lost its activity by approximatively 74 % at the end of 120 min processing time.
Modelling studies were performed to determine the kinetics of hydrolysis, solubilization and enzyme inactivation. The relationship between hydrolysis and solubilization was found linear for all experimental conditions examined. The inactivation energy of
Alcalase at the temperature range of 40–55 °C was determined to be 67.86 kJ mol–1.
Key words:
Corn gluten, Alcalase, hydrolysis, solubilization, modelling sorptio(n): söï thaám huùt beà maët

Introduction
Over the last decade, the use of plant protein hydrolysates in human nutrition has broadly expanded. They are often used in different nutritional formulations, such as supplementation of drinks to enhance their nutritional and functional properties, or special

References: 48 (10) (1994) 77. J., Process Biochemistry 39 (2004) 989. Elsevier Applied Science Publishers, London and New York, 1986. 4. Adler-Nissen, J., J. Agric. Food Chem. 24 (1976) 1090. 6. Adler Nissen, J., Hydrolysis of soy protein. US Patent 4,100,024 (1978). 7. Adler Nissen, J., Ann. Nutr. Alim. 32 (1978) 216. 8. Lee, J. Y., Lee, H. D., Lee, C. H., Food Research International 34 (2001) 217. 16 (2002) 31. (1998) 71. 12. Soral-Smietana, M., Swigon, R., Amarowicz, R., Sijtsma, L., Nahrung 42 (1998) 217. 13. Moreno, M. M. C., Cuadrado, F. V., Process Biochemistry 28 (1993) 481. 14. Raymundo, A., Empis, J., Sousa, I., Food Reaserch and Technology 207 (2) (1998) 91. 15. Lqari, H., Pedroche, J., Giron-Calle, J., Vioque, J., Millan, F., GRASAS Y ACEITES 56 (2) (2005) 135. 16. Drago, S. R., Gonzalez, R. J., Innovative Food Science & Emerging Technologies 1 (2001) 269. 17. Kong, X., Zhou, H., Qian H., Food Chemistry 101 (2007) 615. 18. Popineau, Y., Huchet, B., Larre, C., Berot, S., Journal of Cereal Science 35 (2002) 327. u-Technol. 30 (1997) 441. 20. Friedman, M., Agric. Food Chem. 44 (1996) 6. 21. Hardwick, J. E., Glatz, C. E., J. Agric. Food Chem. 37 (1989) 1188. O., Process Biochemistry 38 (2003) 1239. Technol. 218 (2004) 133. J., J. Biol. Chem. 193 (1951) 265. 25. Lamas, E., Barros, R., Balcao, V., Malcata, F. X., Enzyme and Microbial Technology 28 (2001) 642. 26. Tomarelli, R., Charney, M., Harding, M., Journal of Laboratory Clinical Medicine 34 (1949) 428. 28. Barros, R. M., Malcata, F. X., Food Chemistry 88 (2004) 351. 29. O’Meara, G. M., Munro, P. A., Biotechnol. and Bioeng. 27 (1985) 861. 30. Marquez, M. C., Vazquez, M. A., Process Biochemistry 35 (1999) 111. 31. Margot, A., Flaschel, E., Renken, A., Process Biochemistry 32 (1997) 217. Eng. 2 (2004) 147. C., Enzyme and Microbial Technol. 36 (2005) 555. 34. Sadana, A., Henley, J. P., Biotechnol. and Bioeng. 30 (1987) 717.