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投稿时间:2019-03-31
投稿时间:2019-03-31
中文摘要: 鸡卵类黏蛋白(hen's egg ovomucoid,HOVM)是存在于鸡蛋卵清中的一种致敏蛋白,而热处理是常用的一种蛋制品的加工方式。通过间接酶联免疫吸附测定(enzyme-linked immunosorbent assay,ELISA)法、圆二色谱法、8-苯胺-1-萘磺酸(8-anilino-1-naphthalenesulfonic acid,ANS)荧光探针法以及相关性分析法解释热处理对HOVM 与免疫球蛋白G(immunoglobulin G,IgG)结合能力和结构的影响。结果表明:随着热处理强度(包括温度和时间)的增加,HOVM与IgG 的结合能力不断下降,二级结构中的α-螺旋和β-折叠含量呈下降趋势,β-转角和无规则卷曲的含量呈上升趋势,表面疏水性指数在处理强度较低的情况下会提高,处理强度较高的情况下会下降,HOVM 结合ANS 后的最大荧光波长数(λmax)出现蓝移以及数值变化显示HOVM 结构在热处理的作用下先变得松散,随后处理温度的攀升可能会进一步导致HOVM 蛋白发生凝聚。
Abstract:Hen-egg ovomucoid is an allergenic protein from hen-egg white,and heating treatment is commonly used as a processing method for egg products.Indirect enzyme-linked immunosorbent assay(ELISA),circular dichroism,8-anilino-1-naphthalenesulfonic acid(ANS)fluorescent probe method and relativity analysis were utilized to evaluate effects of heating treatment on the HOVM structure and its ability to bind IgG.Results showed that with the rise of the heat treatment intensity (including heating temperature and heating time),HOVM's ability to bind IgG declined,the content of α-helix and β-sheet secondary structure decreased,and the content of β-turn and random coil increased;Surface hydrophobicity index would increase with treatment intensity being lower and decrease with treatment intensity being higher.When HOVM binding ANS probe,Blue-shift and value variation of the maximum fluorescence wavelength (λmax)revealed that under the heating treatment the protein structure of HOVM became loose,and subsequently higher processing temperature would further cause aggregation of HOVM protein.
keywords: hen's egg ovomucoid(HOVM) indirect enzyme-linked immunosorbent assay(ELISA) circular dichroism 8-anilino-1-naphthalenesulfonic acid(ANS)fluorescent probe surface hydrophobicity secondary structure
文章编号:201913030 中图分类号: 文献标志码:
基金项目:国家自然科学基金项目(31271841);天津市应用基础与前沿技术研究计划面上项目(14JCYBJC30900)
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