Conformation Analysis of Soybean Protein in Reverse Micelles by Circular Dichroism Spectroscopy
文献类型: 外文期刊
作者: Zhao, Xiaoyan 1 ; Ao, Qiang 2 ; Du, Fangling 1 ; Zhu, Qingjun 1 ;
作者机构: 1.Shandong Acad Agr Sci, Inst Agrofood Sci & Technol, Jinan 250100, Peoples R China
2.Tsinghua Univ, Inst Neurol Disorders, Beijing 100049, Peoples R China
关键词: Soybean flour;Reverse micelles;Salts;Soybean protein;CD spectra;Protein secondary structure
期刊名称:FOOD ANALYTICAL METHODS ( 影响因子:3.366; 五年影响因子:3.07 )
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年卷期:
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收录情况: SCI
摘要: Far-UV circular dichroism (CD) spectroscopy was used to study the conformation of protein from soybean flour under the influence of various reverse micelle environments and salt treatments, as compared with the protein using aqueous buffer extraction.These proteins exhibited characteristic CD spectra that reflected a considerable amount of residual secondary structures. The CD analysis showed that the protein modification by reverse micellar system was related to loss of alpha-helix and beta -structure and increase of random coil. The ellipticity of protein in bis (2-ethylhexyl) sodium sulfo-succinate (AOT) and sodium dodecyl sulfate (SDS) reverse micelles was higher than in hexadecyl trimethyl ammonium bromide (CTAB) and TrionX-100. The CD spectrain reverse micelles except for SDS at 210 nm had lower intensity than in aqueous solution. Salts could influence the ellipticity of protein at near 194 nm in an order of NaCl>KNO_3>KCl>NaNO_3>Na_2SO_4 in monovalent salts and in MgCl_2>BaCl_2>CaCl_2 divalent ones. Besides, the ellipticity was totally higher in monovalent salts than in divalent ones.
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