ISSN: 0256-1115 (print version) ISSN: 1975-7220 (electronic version)
Copyright © 2024 KICHE. All rights reserved

Articles & Issues

Language
English
Conflict of Interest
In relation to this article, we declare that there is no conflict of interest.
Publication history
Received March 22, 2010
Accepted April 30, 2010
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Copyright © KIChE. All rights reserved.

All issues

Sesame cake protein hydrolysis by alcalase: Effects of process parameters on hydrolysis, solubilisation, and enzyme inactivation

Department of Chemical Engineering, Davutpaþa Campus, Yildiz Technical University, 34210, Esenler/Istanbul, Turkey
Korean Journal of Chemical Engineering, January 2011, 28(1), 195-202(8), 10.1007/s11814-010-0316-2
downloadDownload PDF

Abstract

We investigated the effects of process parameters (substrate concentration, enzyme concentration, temperature and pH) on the hydrolysis and solubilization of sesame cake protein as well as enzyme stability. The sesame cake protein 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_x000D_ solubilization were obtained as 15 g L^(-1) substrate concentration, 3 ml L^(-1) enzyme concentration, 50 ℃ and pH 8.5. Under these conditions, the values of degree of hydrolysis and solubilization were found as 26.3% and 82.1%, respectively, and enzyme lost its activity by approx. 56% at the end of 120 min processing time. Modeling 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 45-55 ℃ was determined to be 25544 J mol^(-1).

References

Khalid EK, Babiker EE, El AH, Food Chem., 82, 361 (2003)
Nouri L, Legrand J, Popineau Y, Belleville P, Chem. Eng. J., 65(3), 187 (1997)
Schmidl MK, Taylor SL, Nordlee JA, Food Technol., 48(10), 77 (1994)
Bandyopadhyay K, Ghosh S, J. Agric. Food Chem., 50, 6854 (2002)
Chabanon G, Chevalot I, Framboisier X, Chenue S, Marc I, Process Biochem., 42, 1419 (2007)
Kim JM, Whang JH, Kim KM, Koh JH, Suh HJ, Process Biochem., 39, 989 (2004)
Alder-Nissen J, Enzymic hydrolysis of food Proteins. Elsevier Applied Science Publishers, London and New York (1986)
Alder-Nissen J, J. Agric. Food Chem., 24, 1090 (1976)
Apar DK, Oezbek B, J. Chem. Technol. Biotechnol., 82(12), 1107 (2007)
Constantinides A, Adu-Amankwa B, Biotechnol. Bioeng., 22, 1543 (1980)
Adler Nissen J, US Patent, 4,100,024 (1978)
Lee JY, Lee HD, Lee CH, Food Res. Int., 34, 217 (2001)
Karamac M, Amarowicz C, Kostyra H, Czech J. Food Sci., 20, 1 (2002)
Marquez MC, Fernandez V, Chem. Biochem. Eng. Q., 16, 31 (2002)
Periago JM, Vidal LM, Ros G, Rincon F, Martinez C, Lopez G, Rodrigo J, Martinez I, Food Chem., 63, 71 (1998)
Soral-Smietana M, Swigon R, Amarowicz R, Sijtsma L, Nahrung., 42, 217 (1998)
Moreno MMC, Cuadrado FV, Process Biochem., 28, 481 (1993)
Raymundo A, Empis J, Sousa I, Food Res. Technol., 207, 91 (1998)
Lqari H, Pedroche J, Giron-Calle J, Vioque J, Millan F, Grasas Y. Aceites., 56(2), 135 (2005)
Drago SR, Gonzalez RJ, Innovative Food Sci. Emerg. Technol., 1, 269 (2001)
Kong X, Zhou H, Qian H, Food Chem., 101, 615 (2007)
Apar DK, Ozbek B, Chem. Biochem. Eng. Q., 22(2), 203 (2008)
Escamilla-Silva EM, Guzman-Maldonado SH, Cano-Medinal A, Gonzalez-Alatorre G, J. Sci. Food Agric., 83, 972 (2003)
Toshihiko Osawa A, Keiko Nagai O and Kyoko Shibuya N, US Patent, 5,993,795 (1999)
Perez C, Saad R, Archivos Latinoamericanos De Nutrition., 34(4), 735 (1984)
Taha FS, Ibrahim MA, El-Zanaty EA, Grasa y Aceites., 53(3), 267 (2002)
Gonzaleztello P, Camacho F, Jurado E, Paez MP, Guadix EM, Biotechnol. Bioeng., 44(4), 523 (1994)
Lowry OH, Rosebrough NJ, Farr AL, Randall RJ, J. Biol.Chem., 193, 265 (1951)
Lamas EM, Barros RM, Balcao VM, Malcata FX, Enzyme Microb. Technol., 28(7-8), 642 (2001)
Tomarelli R, Charney M, Harding M, J. Lab. Clin. Med., 34, 428 (1949)
Barros RM, Malcata FX, Food Chem., 88, 351 (2004)
O’Meara GM, Munro PA, Biotechnol. Bioeng., 27, 861 (1985)
Marquez MC, Vazquez MA, Process Biochem., 35(1), 111 (1999)
Margot A, Flaschel E, Renken A, Process Biochem., 32(3), 217 (1997)
Sousa R, Lopes GP, Tardioli PW, Giordano RLC, Almeida PIF, Giordano RC, Brazilian J. Chem. Eng., 2, 147 (2004)
Tardioli PW, Sousa RS, Giordano RC, Giordano RLC, Enzyme Microb. Technol., 36(4), 555 (2005)
Bombara N, Anon MC, Pilosof AMR, Lebensm.-Wiss. u- Technol., 30, 441 (1997)
Sadana A, Henley JP, Biotechnol. Bioeng., 30, 717 (1987)

The Korean Institute of Chemical Engineers. F5, 119, Anam-ro, Seongbuk-gu, 233 Spring Street Seoul 02856, South Korea.
TEL. No. +82-2-458-3078FAX No. +82-507-804-0669E-mail : kiche@kiche.or.kr

Copyright (C) KICHE.all rights reserved.

- Korean Journal of Chemical Engineering 상단으로