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Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice
Zhao, Qiang ; Selomulya, Cordelia ; Xiong, Hua ; Chen, Xiao Dong ; Ruan, Xia ; Wang, Shenqi ; Xie, Jianhua ; Peng, Hailong ; Sun, Wenjing ; Zhou, Qiang ; Chen XD(陈晓东)
刊名http://dx.doi.org/10.1016/j.jcs.2012.08.012
2012-11
关键词HIGH-PRESSURE TREATMENT PHYSICOCHEMICAL PROPERTIES SECONDARY STRUCTURE ENDOSPERM PROTEINS FOOD PROTEINS ISOLATE AGGREGATION EXTRACTION SPECTROSCOPY GLOBULIN
英文摘要National Natural Science Foundation of China [21266020]; Programs of State Key Laboratory of Food Science and Technology of Nanchang University [SKLF-KF-201006, SKLF-MB-201005]; Key Program for Oil Processing & Quality Control of the Department of Science and Technology [Gankefa 2010J217]; Graduate Innovative Research Program [YC09A031]; Science and Technology Platform Construction Program [2010DTZ01900]; Leading Technological Innovation Team Program of Jiangxi province [Gankefa 2010J156]; Rice proteins, as a cheap plant protein source from the by-products of rice dreg processing, could potentially replace commonly used proteins such as soy and whey proteins in selected food products. In this study, the functional properties, surface hydrophobicity (H-0), sulfhydryl and disulfide bond contents, thermal properties, as well as secondary structures of native rice endosperm protein (REP) and processed rice dreg protein (RDP) extracted from long-grain indica rice, were compared. RDP was found to have a higher solubility associated with its relatively higher emulsifying and foaming properties than REP, as well as its water/oil holding capacity, although it was a denatured protein. The emulsifying properties were dependent on the solubility and H-0, while solubility was also related to the disulfide bond contents. Distinct differences in H-0, thermal properties, and disulfide bond contents between REP and RDP could be due to the conformational changes, as the industrial processing steps in the production of rice syrups caused an increase in beta-turns at the expense of beta-sheets and random coils of REP, leading to the unfolding of beta-sheets into higher-ordered supramolecular structures for RDP, which could be responsible for its better functional properties. (C) 2012 Elsevier Ltd. All rights reserved.
语种英语
出版者J CEREAL SCI
内容类型期刊论文
源URL[http://dspace.xmu.edu.cn/handle/2288/88376]  
专题化学化工-已发表论文
推荐引用方式
GB/T 7714
Zhao, Qiang,Selomulya, Cordelia,Xiong, Hua,et al. Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice[J]. http://dx.doi.org/10.1016/j.jcs.2012.08.012,2012.
APA Zhao, Qiang.,Selomulya, Cordelia.,Xiong, Hua.,Chen, Xiao Dong.,Ruan, Xia.,...&陈晓东.(2012).Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice.http://dx.doi.org/10.1016/j.jcs.2012.08.012.
MLA Zhao, Qiang,et al."Comparison of functional and structural properties of native and industrial process-modified proteins from long-grain indica rice".http://dx.doi.org/10.1016/j.jcs.2012.08.012 (2012).
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