Effects of Acid-precipitation at Different pH by 3 Kind of Organic Acids on the Structure of Rice Bran Protein

Abstract

Abstract: Compared with hydrochloric acid used in traditional alkaline-extraction and acid-precipitation method, rice bran protein was prepared by the acid-precipitation at condition of tartaric acid, malic acid, and citric acid at pH of 4.0, 3.5, 3.0, and 2.0, respectively. Effects of acid-precipitation by organic acids on structural characteristics of rice bran protein were investigated. The results indicated that when the same organic acid was used to acid-precipitate at different pH, as acid-precipitation pH value decreased, total sulphydryl and α-helix content of rice bran protein changed insignificantly, free sulphydryl and random coil content gradually increased, β-sheet and β-turn content decreased, intrinsic fluorescence intensity and surface hydrophobicity of rice bran protein firstly increased, then decreased. There was no significant difference in total sulphydryl, secondary structure composition, and surface hydrophobicity of rice bran protein between hydrochloric acid and organic acids acid-precipitation at the same pH. Compared with hydrochloric acid, rice bran protein which acid-precipitation by organic acids had lower free sulphydryl content and higher intrinsic fluorescence intensity. The results of molecular weight distribution, particle size distribution, and electrophoresis indicated that acid-precipitation at low pH resulted in partial dissociation and aggregation of rice bran protein, but not form new subunits and high molecular weight aggregates.

Key words: rice bran protein, organic acid, acid-precipitation, structural characteristics

CLC Number:

TS210.9

Wei WU. Effects of Acid-precipitation at Different pH by 3 Kind of Organic Acids on the Structure of Rice Bran Protein[J]. FOOD SCIENCE, 2018, 39(16): 0-0.

References

[1] 吕飞, 许宙, 程云辉. 米糠蛋白提取及其应用研究进展[J]. 食品与机械, 2014, 30(3): 234-238. DOI:10.3969/j.issn. 1003-5788. 2014.03.056.
[2] GUL A, YOUSUF B, SINGH A K，et al. Rice bran: Nutritional values and its emerging potential for development of functional food-A review[J]. Bioactive Carbohydrates and Dietary Fibre, 2015, 6(1):24-30. DOI:10.1016/j.bcdf.2015.06.002.
[3] 肖信锦, 李阳洋, 钟盛华. 米糠中油脂与蛋白提取技术研究进展[J]. 粮食与油脂, 2016, 29(3): 1-4.
[4] 张敏, 周梅, 王长远. 米糠4种蛋白质的提取与功能性质[J]. 食品科学, 2013, 34(1):18-21.
[5] 田阳, 魏帅, 魏益民,等. 稻谷加工产物的镉含量及累积量分析[J]. 中国食品学报, 2014, 14(5): 186-191.
DOI: 10.16429/j.1009-7848.2014.05.032
[6] 丁竹红, 胡忻, 尹大强. 螯合剂在重金属污染土壤修复中应用研究进展[J]. 生态环境学报, 2009, 18(2): 777-782.
[7] 杨滔滔, 李青, 阴开瑞, 等. 酸沉条件对米糠蛋白镉含量和功能性质的影响[J]. 中国油脂, 2016, 41(8): 18-22.
[8] UTSUMI S, MARUYAMA N, SATOH R, et al. Structure-function relationships of soybean proteins revealed by using recombinant systems[J]. Enzyme & Microbial Technology, 2002, 30(3): 284-288. DOI: org/10.1016/S0141-0229(01)00507-5
[9] CHANDI G K, SOGI D S. Functional properties of rice bran protein concentrates[J]. Journal of Food Engineering, 2007, 79(2): 592-597. DOI: org/10.1016/j.jfoodeng.2006.02.018
[10] ZHANG H J, ZHANG H, WANG L, et al. Preparation and functional properties of rice bran proteins from heat-stabilized defatted rice bran[J]. Food Research International, 2012, 47(2): 359-363. DOI: org/10.1016/j.foodres.2011.08.014
[11] HUANG Y R, HUA Y F, QIU A Y. Soybean protein aggregation induced by lipoxygenase catalyzed linoleic acid oxidation [J]. Food Research International, 2006, 39(2): 240-249. DOI:10.1016/j.foodres.2005.07.012
[12] LIU Y, ZHAO G L, ZHAO M M, et al. Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction[J]. Journal of Food Chemistry, 2012, 131(3): 901-906. DOI: org/10.1016/j.foodchem.2011.09.074
[13] PUPPO M C, ANON M C. Soybean protein dispersions at acid pH.Thermal and rheological properties[J]. Journal of Food Science, 1999, 64(1): 50-56. DOI: 10.1111/j.1365-2621.1999.tb09859.x
[14] FANG Y Q, ZHANG B, WEI Y M, et al. Effects of specific mechanical energy on soy protein aggregation during extrusion process studied by size exclusion chromatography coupled with multiangle laser light scattering[J]. Journal of Food Engineering, 2013, 115: 220-225. DOI: org/10.1016/j.jfoodeng.2012.10.017
[15] WU W, WU X J, HUA Y F. Structural modification of soy protein by the lipid peroxidation product acrolein[J]. LWT-Food Science and Technology, 2010, 43(1):133-140. DOI: 10.1002/jsfa.3606
[16] JIANG J, CHEN J, XIONG Y L. Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes[J]. Journal of Agricultural & Food Chemistry, 2009, 57(16):7576-83. DOI: 10.1021/jf901585n
[17] JIANG J, XIONG Y L, CHEN J. Role of β-conglycinin and glycinin subunits in the pH-shifting induced structural and physicochemical changes of soy protein isolate[J]. Journal of Food Science, 2011, 76(2): 293-302. DOI: 10.1111/j.1750-3841.2010.02035.x
[18] LIU Q, GENG R, ZHAO J, et al. Structural and gel textural properties of soy protein isolate when subjected to extreme acid pH-Shifting and mild heating processes[J]. Journal of Agricultural & Food Chemistry, 2015, 63(19): 4853–4861. DOI: 10.1021/acs.jafc.5b01331
[19] 王长远, 郝天舒, 张敏. 干热处理对米糠蛋白结构与功能特性的影响[J]. 食品科学, 2015, 36(7): 13-18. DOI:10.7506/spkx1002-6630-201507003
[20] 赵谋明, 源博恩, 罗东辉, 等. 酸性条件下大豆分离蛋白的亚基解离[J]. 华南理工大学学报(自然科学版): 2011, 39(9): 22-27. DOI: 10.3969/j.issn.1000-565X.2011.09.005
[21] JIANG J, XIONG Y L. Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase[J]. Meat Science, 2013, 93(3): 469-476. DOI: org/10.1016/j.meatsci.2012.11.002
[22] DONG X, ZHAO M, YANG B, et al. Effect of high-pressure homogenization on the functional property of peanut protein[J]. Journal of Food Process Engineering, 2011, 34(34):2191-2204. DOI: 10.1111/j.1745-4530.2009.00546.x
[23] KRISTINSSON H G, HULTIN H O. Changes in conformation and subunit assembly of cod myosin at low and high pH and after subsequent refolding [J]. Journal of Agricultural and Food Chemistry, 2003, 51(24): 7187-7196. DOI: 10.1021/jf026193m
[24] 赵谋明, 辛佩贤, 赵强忠,等. 酸性条件下花生分离蛋白亚基结构的变化规律[J]. 现代食品科技, 2014,30(12):37-42. DOI: 10.13982/j.mfst.1673-9078.2014.12.007
[25] AROGUNDADE L A, TSHAY M, SHUMEY D, et al. Effect of ionic strength and/or pH on extractability and physico functional characterization of broad bean ( Vicia faba L.) protein concentrate [J]. Food Hydrocolloids, 2006, 20 (8): 1124-1134. DOI: org/10.1016/j.foodhyd.2005.12.010
[26] 吴伟, 蔡勇建, 吴晓娟, 等. 米糠贮藏过程中清蛋白结构变化的研究[J]. 中国油脂, 2016, 41(7): 15-20.
[27] LAKEMOND C M M, JONGH H H J D, HESSING M, et al. Soy glycinin: influence of pH and ionic strength on solubility and molecular structure at ambient temperatures[J]. Journal of Agricultural & Food Chemistry, 2000, 48(6): 1985-90. DOI: 10.1021/jf9908695
[28] 魏冬旭, 江连洲, 王辰, 等. pH值对大豆11S球蛋白结构和表面疏水性的影响[J]. 食品科学, 2015, 36(11): 1-5. DOI: 10.7506/spkx1002-6630-201511001
[29] 源博恩, 赵强忠, 赵谋明. 酸性条件下高压均质对大豆蛋白结构与功能特性的影响[J]. 食品工业科技, 2012, 33(8):117-120.
[30] WAGNER J R, D A SORGENTINI, M CA?ón. Thermal and electrophoretic behavior, hydrophobicity, and Some functional properties of acid-treated soy isolates[J]. Journal of Agricultural & Food Chemistry, 1996, 44(7): 1881-1889. DOI: 10.1021/jf950444s
[31] ZHANG Y H, HUANG L H. Effect of heat-induced formation of rice bran protein fibrils on morphological structure and physicochemical properties in solutions and gels[J]. Food Science and Biotechnology, 2014, 23(5): 1417-1423. DOI: 10.1007/s10068-014-0194-1