OPTIMIZATION OF LIMITED HYDROLYSIS OF PROTEINS IN RICE RESIDUE AND CHARACTERIZATION OF THE FUNCTIONAL PROPERTIES OF THE PRODUCTS
2012; Wiley; Volume: 37; Issue: 3 Linguagem: Inglês
10.1111/j.1745-4549.2011.00641.x
ISSN1745-4549
AutoresXingfeng Guo, Juanjuan Zhang, Yu‐Xiang Ma, Shaojun Tian,
Tópico(s)Biochemical effects in animals
ResumoJournal of Food Processing and PreservationVolume 37, Issue 3 p. 245-253 Original Article OPTIMIZATION OF LIMITED HYDROLYSIS OF PROTEINS IN RICE RESIDUE AND CHARACTERIZATION OF THE FUNCTIONAL PROPERTIES OF THE PRODUCTS XINGFENG GUO, XINGFENG GUO School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorJUANJUAN ZHANG, JUANJUAN ZHANG School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorYUXIANG MA, YUXIANG MA School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorSHAOJUN TIAN, Corresponding Author SHAOJUN TIAN School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, China TEL: +861-371-67756823; FAX: 861-371-67756823; EMAIL: [email protected]Search for more papers by this author XINGFENG GUO, XINGFENG GUO School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorJUANJUAN ZHANG, JUANJUAN ZHANG School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorYUXIANG MA, YUXIANG MA School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, ChinaSearch for more papers by this authorSHAOJUN TIAN, Corresponding Author SHAOJUN TIAN School of Food Science and Technology, Henan University of Technology, Songshan Road 140, ZhengZhou 450052, China TEL: +861-371-67756823; FAX: 861-371-67756823; EMAIL: [email protected]Search for more papers by this author First published: 05 March 2012 https://doi.org/10.1111/j.1745-4549.2011.00641.xCitations: 23Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Abstract ABSTRACT Four enzymes, alcalase, neutrase, bromelain and papain, were used individually to hydrolyze proteins in rice residue. The process conditions were optimized by response surface methodology (RSM). Under optimal conditions hydrolyzate yields generated with neutrase, alcalase, bromelain and papain were 49.3, 56.7, 30.8 and 16.6%, respectively. Molecular weight distributions of the hydrolyzates were analyzed by high-performance liquid chromatography. The results showed that hydrolyzate generated with neutrase and alcalase had smaller polypeptides than those with bromelain and papain. Compared with alkaline extraction, the solubility of the hydrolyzates treated by enzyme was greatly improved. Antioxidant activities of the hydrolyzates were also evaluated in this study. The induction time of the hydrolyzate generated with alcalase was longer than those with other enzymes. Emulsifying activities of the hydrolyzates generated with different enzymes were significantly different and that prepared with alcalase exhibited the best emulsifying activity among all other hydrolyzates. PRACTICAL APPLICATIONS Rice residue is a by-product of extracting starch and other carbohydrates from rice. The residue is rich in protein, but is normally used as animal feed because of the poor solubility. In this research, alcalase, neutrase, bromelain and papain were used individually to hydrolyze proteins in rice residue. RSM was used to establish models to estimate the optimum conditions and predict the hydrolyzate yield at different conditions. Under the optimum conditions, hydrolyzates were prepared and the functional properties of the products generated with different enzymes and extracted by alkaline were compared. The solubility and other properties of rice protein hydrolyzates were greatly improved, so it could be used for nutritional supplementing, functional enhancement, etc. Therefore, this article has practical value, which provided the theoretical basis for the application of rice residue. This text should highlight the uses of rice residue, either actual or potential. REFERENCES ADEBIYI, A.P., ADEBIYI, A.O., HASEGAWA, Y., OGAWA, T. and MURAMOTO, K. 2009a. Isolation and characterization of protein fractions from deoiled rice bran. Eur. Food Res. Technol. 228, 391– 401. ADEBIYI, A.P., ADEBIYI, A.O., YAMASHITA, J., OGAWA, T. and MURAMOTO, K. 2009b. Purification and characterization of antioxidative peptides derived from rice bran protein hydrolysates. Eur. Food Res. Technol. 228, 553– 563. ADLER-NISSEN, J. 1986. Enzymic Hydrolysis of Food Proteins, Elsevier Applied Science, New York, NY. ANDERSON, A., HETTIARACHCHY, N. and JU, Z.Y. 2001. Physicochemical properties of pronase-treated rice glutelin. J. Am. Oil Chem. Soc. 78, 1– 6. CAO, X., WEN, H., LI, C. and GU, Z. 2009. Differences in functional properties and biochemical characteristics of congenetic rice proteins. J. Cereal Sci. 50, 184– 189. CHANG, K.C., LEE, C.C. and BROWN, G. 1986. Production and nutritional evaluation of a high-protein rice flour. J. Food Sci. 51, 464– 467. CHEL-GUERRERO, L., PREZ-FLORES, V., BETANCUR-ANCONA, D. and DVILA-ORTIZ, G. 2002. Functional properties of flours and protein isolates from Phaseolus lunatus and Canavalia ensiformis seeds. J. Agric. Food Chem. 50, 584– 591. CHEN, Y.-J., CHEN, Y.-Y., WU, C.-T., YU, C.-C. and LIAO, H.-F. 2010. Prolamin, a rice protein, augments anti-leukaemia immune response. J. Cereal Sci. 51, 189– 197. DEVI, R.R. and ARUMUGHAN, C. 2007. Phytochemical characterization of defatted rice bran and optimization of a process for their extraction and enrichment. Bioresour. Technol. 98, 3037– 3043. FABIAN, C.B., HUYNH, L.H. and JU, Y.H. 2010. Precipitation of rice bran protein using carrageenan and alginate. LWT – Food Sci. Technol. 43, 375– 379. FIOCCHI, A., TRAVAINI, M., D'AURIA, E., BANDERALI, G., BERNARDO, L. and RIVA, E. 2003. Tolerance to a rice hydrolysate formula in children allergic to cow's milk and soy. Clin. Exp. Allergy 33, 1576– 1580. GORTZI, O., LALAS, S., CHINOU, I. and TSAKNIS, J. 2008. Reevaluation of bioactivity and antioxidant activity of Myrtus communis extract before and after encapsulation in liposomes. Eur. Food Res. Technol. 226, 583– 590. HAMADA, J.S. 1997. Characterization of protein fractions of rice bran to devise effective methods of protein solubilization. Cereal Chem. 74, 662– 668. HAMADA, J.S. 2000. Characterization and functional properties of rice bran proteins modified by commercial exoproteases and endoproteases. J. Food Sci. 65, 305– 309. HANMOUNGJAI, P., PYLE, D.L. and NIRANJAN, K. 2001. Enzymatic process for extracting oil and protein from rice bran. J. Am. Oil Chem. Soc. 78, 817– 821. HATA, S., WIBOONSIRIKUL, J., MAED, A., KIMURA, Y. and ADACHI, S. 2008. Extraction of defatted rice bran by subcritical water treatment. Biochem. Eng. J. 40, 44– 53. HERNANDEZ, N., RODRIGUEZ-ALEGRÍA, M.E., GONZALEZ, F. and LOPEZ-MUNGUIA, A. 2000. Enzymatic treatment of rice bran to improve processing. J. Am. Oil Chem. Soc. 77, 177– 180. KAEWKA, K., THERAKULKAIT, C. and CADWALLADER, K.R. 2009. Effect of preparation conditions on composition and sensory aroma characteristics of acid hydrolyzed rice bran protein concentrate. J. Cereal Sci. 50, 56– 60. KIRALAN, M., BAYRAK, A. and ÖZKAYA, M.T. 2009. Oxidation stability of virgin olive oils from some important cultivars in East Mediterranean Area in Turkey. J. Am. Oil Chem. Soc. 86, 247– 252. MUJOO, R., CHANDRASHEKAR, A. and ALI, S.Z. 1998. Rice protein aggregation during the flaking process. J. Cereal Sci. 28, 187– 195. OSZVALD, M., TÖMÖSKÖZI, S., LARROQUE, O., KERESZTÉYI, E., TAMÁSD, L. and BÉKÉS, F. 2008. Characterization of rice storage proteins by SE-HPLC and micro z-arm mixer. J. Cereal Sci. 48, 68– 76. PARAMAN, I., HETTIARACHCHY, N.S., SCHAEFER, C. and BECK, M.I. 2006. Physicochemical properties of rice endosperm proteins extracted by chemical and enzymatic methods. Cereal Chem. 83, 663– 667. PARAMAN, I., HETTIARACHCHY, N.S. and SCHAEFER, C. 2007a. Glycosylation and deamidation of rice endosperm protein for improved solubility and emulsifying properties. Cereal Chem. 84, 593– 599. PARAMAN, I., HETTIARACHCHY, N.S., SCHAEFER, C. and BECK, M.I. 2007b. Hydrophobicity, solubility, and emulsifying properties of enzyme-modified rice endosperm protein. Cereal Chem. 84, 343– 349. PARAMAN, I., HETTIARACHCHY, N.S. and SCHAEFER, C. 2008. Preparation of rice endosperm protein isolate by alkali extraction. Cereal Chem. 85, 76– 81. PARRADO, J., MIRAMONTES, E., JOVER, M., GUTIERREZ, J.F., TERÁN, L.C. and BAUTISTA, J. 2006. Preparation of a rice bran enzymatic extract with potential use as functional food. Food Chem. 98, 742– 748. SCHWENKE, K.D. 1997. Enzyme and chemical modification of proteins. In Food Proteins and Their Applications ( S. Damodaran and A. Paraf, eds.) p. 395, Marcel Dekker, New York, NY. SEREEWATTHANAWUT, I., PRAPINTIP, S., WATCHIRARUJI, K., GOTO, M., SASAKI, M. and SHOTIPRUK, A. 2008. Extraction of protein and amino acids from deoiled rice bran by subcritical water hydrolysis. Bioresour. Technol. 99, 555– 561. SHIH, F.F. and DAIGLE, K. 1997. Use of enzymes for the separation of protein from rice flour. Cereal Chem. 74, 437– 441. SHIH, F.F. and DAIGLE, K.W. 2000. Preparation and characterization of rice protein isolates. J. Am. Oil Chem. Soc. 77, 885– 889. SHIM, S.-Y., KATAKURA, Y., ICHIKAWA, A., TERUYA, K., MATSUDA, T. and SHIRAHATA, S. 2001. Epitope analysis of human monoclonal antibody specific for rice allergenic protein generated by in vitro immunization. Cytotechnology 36, 109– 115. TOMPSON, D. 1982. Response surface experimentation. J. Food Process. Preserv. 6, 155– 188. YIN, H., FAN, G. and GU, Z. 2010. Optimization of culture parameters of selenium-enriched yeast (Saccharomyces cerevisiae) by response surface methodology (RSM). LWT – Food Sci. Technol. 43, 666– 669. ZHANG, W., BI, J., CHEN, L., ZHENG, L., JI, S., XIA, Y., XIE, K., ZHAO, Z., WANG, Y., LIU, L. et al. 2008. QTL mapping for crude protein and protein fraction contents in rice (Oryza sativa L.). J. Cereal Sci. 48, 539– 547. ZHANG, J., ZHANG, H., WANG, L., GUO, X., WANG, X. and YAO, H. 2009. Antioxidant activities of the rice endosperm protein hydrolysate: Identification of the active peptide. Eur. Food Res. Technol. 229, 709– 719. ZHANG, J., ZHANG, H., WANG, L., GUO, X., WANG, X. and YAO, H. 2010. Isolation and identification of antioxidative peptides from rice endosperm protein enzymatic hydrolysate by consecutive chromatography and MALDI-TOF/TOF MS/MS. Food Chem. 119, 226– 234. ZHENG, H.-G., YANG, X.-Q., TANG, C.-H., LI, L. and AHMAD, I. 2008. Preparation of soluble soybean protein aggregates (SSPA) from insoluble soybean protein concentrates (SPC) and its functional properties. Food Res. Intern. 41, 154– 164. Citing Literature Volume37, Issue3June 2013Pages 245-253 ReferencesRelatedInformation
Referência(s)