【作者】 何欣蓉； 刘光宇； 曹敏杰； 刘光明；

【Author】 He Xinrong;Liu Guangyu;Cao Minjie;Liu Guangming;College of Food and Bioscience Engineering,Jimei University;Key laboratory of Marine functional food in Xiamen;Marine functional food engineering technology center of Fujian Province;National Joint Engineering Research Center for deep processing of aquatic products;

【机构】 集美大学食品与生物工程学院； 厦门市海洋功能食品重点实验室； 福建省海洋功能食品工程技术研究中心； 水产品深加工技术国家地方联合工程研究中心；

【摘要】 本研究对章鱼肌肉蛋白35 ku的过敏组分进行分离纯化和理化特性分析。以章鱼肌肉为原料,采用硫酸铵分步盐析、柱层析(DEAE-Sepharose柱层析)进行纯化,利用肽指纹质量图谱对所得蛋白进行鉴定,同时对其热稳定性、pH稳定性及消化稳定性进行分析。结果表明,纯化得到分子量约为35 ku的蛋白,经肽指纹质量图谱鉴定其为章鱼原肌球蛋白(Tropomyosin,TM);不同热处理温度及pH条件下,TM主条带均未发生明显变化;TM在胃蛋白酶作用下,随着时间的延长,TM主条带没有发生明显变化,且主条带下方也没有出现明显的降解条带;在胰蛋白酶作用下,随着时间的延长,TM主条带逐渐变浅最终消失,与0 min相比,反应5 min时开始出现明显的降解条带。理化特性分析表明,TM有很好的热稳定性及pH稳定性;TM不易被胃蛋白酶消化;TM对胰蛋白酶的耐受性较弱,容易被降解。纯化得到的章鱼TM有望用于过敏性疾病的临床检测。更多还原

【Abstract】 In this study,the allergic components of muscle protein 35 ku in octopus were isolated and purified and physicochemical characteristics were analyzed to provide references for the diagnosis and control of allergic diseases.In this experiment,octopus muscle was used as raw material for purification by ammonium sulfate step salting and column chromatography(DEAE-Sepharose column chromatography),and the obtained protein was identified by using the peptide fingerprint mass map.Meanwhile,its thermal stability,pH stability and digestive stability were analyzed.The results showed that the protein whose molecular weight was about 35 ku was purified and identified as Tropomyosin(TM) by the peptide fingerprint mass map.Under different temperature and pH conditions,the TM main bands did not change significantly.Under the action of pepsin,TM’s main bands did not change significantly over time,and there was no obvious degradation band under the main bands.Under the action of trypsin,TM main bands gradually became shallower and finally disappeared with the extension of time.Compared with 0 min,significant degradation bands began to appear at 5 min of reaction.The analysis of physicochemical characterizations shows that TM has good thermal stability and pH stability.TM is not easily digested by pepsin;TM is less tolerant to trypsin and is easily degraded.Purified octopus TM is expected to be used for clinical detection of allergic diseases.更多还原