【作者】 沈海旺； 曹敏杰； 蔡秋凤； 苏文金； 刘光明；

【Author】 Haiwang Shen Minjie Cao Qiufeng Cai Wenjin Su Guangming Liu (School of Biotechnology Engineering,Jimei University,Xiamen 361021,China)

【机构】 集美大学生物工程学院；

【摘要】 目的:通过对章鱼进行不同加工处理,研究章鱼主要过敏原原肌球蛋白(Tropomyosin,TM)的性质变化,优化能有效降低过敏原免疫原性的加工处理条件。方法:通过制作丙酮粉、硫酸铵分级沉淀、DEAE-Sephrose柱层析等方法纯化得到TM,用SDS-PAGE或者western blotting对其温度稳定性、pH稳定性、消化稳定性以及高温高压、紫外和超声等加工处理方式对其消化稳定性的影响进行分析;同时对章鱼肌肉进行同样条件处理,研究其中TM消化稳定性变化;最后采用抑制性酶联免疫吸附实验(I-ELISA)分析模拟胃肠液消化和加工处理对TM致敏性的影响。结果:章鱼TM对温度和pH均比较稳定,对胃蛋白酶有比较强的耐受性,容易被胰蛋白酶和胰凝乳蛋白酶降解;高温高压处理能有效促进TM被消化酶降解,并降低TM的致敏性。更多还原

【Abstract】 Tropomyosin(TM)is the major allergen of octopus(Octopus fangsiao).The aim of this study was to investigate the effect of processing methods on the degradation of TM and reduction of its allergenicity.Methods:Octopus TM was purified by making acetone powder,ammonium sulfate fractionation,and DEAE-Sepharose column chromatography.Temperature stability,pH stability and digestion stability of TM and the effects of different processing methods including high temperature,high pressure,ultraviolet radiation and ultrasonic on TM were analyzed by SDS-PAGE and western blotting. And then,the octopus muscle was processed at the same way,and the digestion stability of TM in the muscle was studied.The allergenicity of TM in different process ways and digested by protease was further identified by inhibitory enzyme-linked immunosorbent assay(I-ELISA).Results:Octopus TM was stable in different temperature and pH,and was hard digested by pepsin,but could be easily digested by trypsin and chymotrypsin.And high temperature and high pressure could promote the degradation of octopus TM,and reduce the allergenicity of octopus TM.更多还原