The physicochemical and structural properties of the concentrated rice bran protein (CRBP) and rice bran protein fractions – RBPF (albumin, globulin, prolamin, and glutelin) were investigated on the basis of multiple solvent extraction method. The protein fractions mainly consisted of essential amino acids except for prolamin. The amino acid composition of concentrated protein was superior to soybean protein isolation, such as valine, methionine, leucine, phenylalanine, and histidine, with similar characteristics of solubility, emulsification, and foaming. Based on the difference in amino acid composition, all these five proteins showed relatively high surface hydrophobicity more than 369.3 of prolamin. CRBP and RBPF were composed of different molecular subunits in SDS-PAGE profile. The circular dichroism spectra (CDS) in synergy showed that the primary structures of RBPF were β-protein folding and random coils with various denaturation temperatures in the range of 78.69°C for glutelin and 92.88°C for globulin. The fluorescence spectrometry assays showed that the blue shift occurred at 348 nm for globulin, while the red shift occurred for the concentrated protein, albumin, and globulin at 356.2, 348.6, and 347.0 nm, respectively. Therefore, the research presents the basic characterisation for further application of natural rice bran protein in the food industry.
Adebiyi Abayomi P., Adebiyi Ayobamitale O., Hasegawa Yusuke, Ogawa Tomohisa, Muramoto Koji (2009): Isolation and characterization of protein fractions from deoiled rice bran. European Food Research and Technology, 228, 391-401
https://doi.org/10.1007/s00217-008-0945-4
Agboola Samson, Ng Darren, Mills Dominic (2005): Characterisation and functional properties of Australian rice protein isolates. Journal of Cereal Science, 41, 283-290
https://doi.org/10.1016/j.jcs.2004.10.007
BERA M. B., MUKHERJEE R. K. (1989): Solubility, Emulsifying, and Foaming Properties of Rice Bran Protein Concentrates. Journal of Food Science, 54, 142-145
https://doi.org/10.1111/j.1365-2621.1989.tb08587.x
E. Chove Bernard, Grandison Alistair S., Lewis Michael J. (2007): Some functional properties of fractionated soy protein isolates obtained by microfiltration. Food Hydrocolloids, 21, 1379-1388
https://doi.org/10.1016/j.foodhyd.2006.10.018
Damodaran S. (1997): Food proteins. a overview. In: Damodaran S., Paraf A. (eds): Food Proteins and their Applications. 1st Ed. New York, Marcel Dekker: 1–21.
Fabian C.B., Huynh L.H., Ju Y.H. (2010): Precipitation of rice bran protein using carrageenan and alginate. LWT - Food Science and Technology, 43, 375-379
https://doi.org/10.1016/j.lwt.2009.08.005
Garciacarreno F.L., Dimes L.E., Haard N.F. (1993): Substrate-Gel Electrophoresis for Composition and Molecular Weight of Proteinases or Proteinaceous Proteinase Inhibitors. Analytical Biochemistry, 214, 65-69
https://doi.org/10.1006/abio.1993.1457
German Bruce, Damodaran Srinivasan, Kinsella John E. (1982): Thermal dissociation and association behavior of soy proteins. Journal of Agricultural and Food Chemistry, 30, 807-811
https://doi.org/10.1021/jf00113a002
GNANASAMBANDAM RAVIN, HElTIARACHCHY N.S. (1995): Protein Concentrates from Unstabilized and Stabilized Rice Bran: Preparation and Properties. Journal of Food Science, 60, 1066-1069
https://doi.org/10.1111/j.1365-2621.1995.tb06293.x
Hamada J. S. (1997): Characterization of Protein Fractions of Rice Bran to Devise Effective Methods of Protein Solubilization. Cereal Chemistry, 74, 662-668
https://doi.org/10.1094/CCHEM.1997.74.5.662
Haskard Carolyn A., Li-Chan Eunice C. Y. (1998): Hydrophobicity of Bovine Serum Albumin and Ovalbumin Determined Using Uncharged (PRODAN) and Anionic (ANS
- ) Fluorescent Probes. Journal of Agricultural and Food Chemistry, 46, 2671-2677
https://doi.org/10.1021/jf970876y
Jiang Shu-Juan, Zhao Xin-Huai (2010): Transglutaminase-induced cross-linking and glucosamine conjugation in soybean protein isolates and its impacts on some functional properties of the products. European Food Research and Technology, 231, 679-689
https://doi.org/10.1007/s00217-010-1319-2
Agyare Kingsley K., Addo Kwaku, Xiong Youling L. (2009): Emulsifying and foaming properties of transglutaminase-treated wheat gluten hydrolysate as influenced by pH, temperature and salt. Food Hydrocolloids, 23, 72-81
https://doi.org/10.1016/j.foodhyd.2007.11.012
Kinsella J (1981): Functional properties of proteins: Possible relationships between structure and function in foams. Food Chemistry, 7, 273-288
https://doi.org/10.1016/0308-8146(81)90033-9
LAEMMLI U. K. (1970): Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4. Nature, 227, 680-685
https://doi.org/10.1038/227680a0
Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. (1951): Protein measurement with the Folin phenol reagent. Journal of Biological Chemistry, 193: 265–275.
Mao Xiaoying, Hua Yufei (2012): Composition, Structure and Functional Properties of Protein Concentrates and Isolates Produced from Walnut (Juglans regia L.). International Journal of Molecular Sciences, 13, 1561-1581
https://doi.org/10.3390/ijms13021561
Mohamed A., Peterson S.C., Hojilla-Evangelista M.P., Sessa D.J., Rayas-Duarte P., Biresaw G. (2004): Effect of heat treatment and pH on the physicochemical properties of lupin protein. Journal of the American Oil Chemists Society, 81: 1153–1157.
Molina Ortiz Sara E, Wagner Jorge R (2002): Hydrolysates of native and modified soy protein isolates: structural characteristics, solubility and foaming properties. Food Research International, 35, 511-518
https://doi.org/10.1016/S0963-9969(01)00149-1
Moure Andrés, Sineiro J., Domínguez Herminia, Parajó Juan Carlos (2006): Functionality of oilseed protein products: A review. Food Research International, 39, 945-963
https://doi.org/10.1016/j.foodres.2006.07.002
Ogunwolu Semiu Olalekan, Henshaw Folake O., Mock Hans-Peter, Santros Andrea, Awonorin Samuel O. (2009): Functional properties of protein concentrates and isolates produced from cashew (Anacardium occidentale L.) nut. Food Chemistry, 115, 852-858
https://doi.org/10.1016/j.foodchem.2009.01.011
Osborne T.B. (1907): The Proteins of the Wheat Kernel. Washington, Carnegie Institution of Washington, 84: 5–119.
Pour-Ei A. (1981): Protein functionality: classification, definition and methodology. In: Cherry J.-P: Protein Functionality in Foods. ACS Symposium Series. Washington: American Chemical Society: 1–19.
Shih F. F., Champagne E. T., Daigle K., Zarins Z. (1999): Use of enzymes in the processing of protein products from rice bran and rice flour. Nahrung / Food, 43, 14-18
https://doi.org/10.1002/(SICI)1521-3803(19990101)43:1<14::AID-FOOD14>3.0.CO;2-K
Singh Narpinder, Kaur Maninder, Sandhu Kawaljit Singh (2005): Physicochemical and Functional Properties of Freeze-Dried and Oven Dried Corn Gluten Meals. Drying Technology, 23, 975-988
https://doi.org/10.1081/DRT-200054253
SNOW S.D., BROOKS J.R. (1989): Fractionation of Rice Glutelin Polypeptides using Gel Filtration Chromatography. Journal of Food Science, 54, 730-733
https://doi.org/10.1111/j.1365-2621.1989.tb04691.x
Sze-Tao K.W.C., Sathe S.K. (2000): Functional properties and in vitro digestibility of almond (Prunus dulcis L.) protein isolate. Food Chemistry, 69, 153-160
https://doi.org/10.1016/S0308-8146(99)00244-7
Tang Chuan-He, Sun Xin (2010): Physicochemical and Structural Properties of 8S and/or 11S Globulins from Mungbean [
Vigna radiata (L.) Wilczek] with Various Polypeptide Constituents. Journal of Agricultural and Food Chemistry, 58, 6395-6402
https://doi.org/10.1021/jf904254f
Tang Shanhu, Hettiarachchy Navam S., Shellhammer Thomas H. (2002): Protein Extraction from Heat-Stabilized Defatted Rice Bran. 1. Physical Processing and Enzyme Treatments. Journal of Agricultural and Food Chemistry, 50, 7444-7448
https://doi.org/10.1021/jf025771w
Wang M., Hettiarachchy N. S., Qi M., Burks W., Siebenmorgen T. (1999): Preparation and Functional Properties of Rice Bran Protein Isolate. Journal of Agricultural and Food Chemistry, 47, 411-416
https://doi.org/10.1021/jf9806964
Wu Wei, Zhang Caimeng, Kong Xiangzhen, Hua Yufei (2009): Oxidative modification of soy protein by peroxyl radicals. Food Chemistry, 116, 295-301
https://doi.org/10.1016/j.foodchem.2009.02.049
Zhang H.-J., Zhang H., Wang L., Guo X.-N. (2012): Preparation and functional properties of rice bran proteins from heat-stabilized defatted rice bran. Food Research International, 47, 359-363
https://doi.org/10.1016/j.foodres.2011.08.014