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作 者:黄群[1,2] 马美湖[1] 蔡朝霞[1] 罗章[1,3] 黄茜[1] 孙术国[1,2]
机构地区:[1]国家蛋品加工技术研发分中心,华中农业大学食品科学技术学院,湖北武汉430070 [2]吉首大学食品科学研究所,湖南吉首416000 [3]西藏农牧学院食品科学学院,西藏林芝860000
出 处:《光谱学与光谱分析》2011年第12期3319-3322,共4页Spectroscopy and Spectral Analysis
基 金:现代农业产业技术体系建设专项资金项目(nycytx-41-g22)资助
摘 要:采用圆二色谱(CD)、X射线衍射(XRD)、ANS荧光探针和紫外光谱(UV)研究了S-构型转化对卵白蛋白微观结构的影响。结果显示,不同诱导时间处理的卵白蛋白二级结构的α-螺旋,β-折叠,β-转角和无规卷曲之间相互转化,α-螺旋略有减少,β-折叠相应增加,分子有序性提高;S-构型转化后卵白蛋白晶体结构增加,72h处理后结晶区最大,说明蛋白结构的有序性提高,与CD分析结果一致;卵白蛋白的表面疏水性随诱导时间的延长而增强,72h处理后达到最大值;S-构型转化使卵白蛋白分子表面具有紫外吸收的芳香氨基酸残基包埋于分子内部,导致最大紫外吸光值随诱导时间的延长而下降。研究表明,卵白蛋白的微观结构变化与S-构型转化有关。The effect of S-configuration transformation on the microstructure of ovalbumin was studied by CD spectra,XRDspectra,ANS fluorescence probe emission spectra and UV absorption spectra.CD spectra was used to examine the changes inthe secondary structure of the ovalbumin during S-ovalbumin information process.When the induction time was prolonged,themutual transformation betweenα-helix,β-sheet,β-turn and the random coil was observed,and the orderliness of the secondarystructure was increased withα-helix decreasing slightly andβ-sheet increasing correspondingly.XRD spectra analysis showedthat the crystal structure content of the ovalbumin increased with prolonging the induction time and the largest data was observedat 72h,indicating that the orderliness of the secondary structure was increased.The results were similar to CD spectra analysis.The ANS fluorescence probe emission spectra analysis demonstrated that S-configuration transformation induced an increase insurface hydrophobicity with prolonging the induction time,and the largest data was also observed at 72h.In addition,UV ab-sorption spectra analysis indicated that S-configuration transformation resulted in a decrease in the UV-absorption maximum val-ue with prolonging the induction time,indicating that the aromatic amino acid was buried in the molecular interior.The resultsindicated that the changes in the microstructure of ovalbumin were relevant to S-configuration transformation.
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