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作 者:胡晓利 布冠好[1] 陈复生[1] HU Xiaoli;BU Guanhao;CHEN Fusheng(College of Food Science and Technology, Henan University of Technology (Zhengzhou 450001))
出 处:《食品工业》2019年第1期130-134,共5页The Food Industry
基 金:河南省科技攻关项目(182102110299);国家自然科学基金项目(31201293);河南省教育厅科学技术研究重点项目(14B550013);河南工业大学省属高校基本科研业务费专项(2015RCJH02)
摘 要:试验以大豆分离蛋白为原料,选择超声波和酶解联合处理大豆蛋白,采用间接竞争ELISA法和免疫印迹法测定大豆主要抗原蛋白β-伴大豆球蛋白的抗原性和免疫活性,并分析超声波和酶解处理后大豆蛋白的结构变化。结果表明,超声波联合酶解处理能够显著降低β-伴大豆球蛋白的抗原性和免疫活性, 400 W、15 min超声波预处理的大豆蛋白质再经酶解处理后,β-伴大豆球蛋白的抗原抑制率降低了61.15%;电泳结果显示,超声波联合酶解处理能够使蛋白质肽键断裂,分解为小分子肽段;表面疏水性结果表明,蛋白质的空间结构发生解聚和重新聚合,三四级结构被破坏,构象型表位可能被改变。β-伴大豆球蛋白的抗原性的变化主要是因为超声波与酶解联合引起大豆蛋白氨基酸序列及空间结构的变化。In this experiment, soy protein isolate was used as raw material, ultrasonic and enzymatic hydrolysis were combined to treat soy protein, and the antigenicity and immunological activity of soybean main antigen protein β-conglycinin were determined by indirect competitive ELISA and immunoblotting. Structural changes in soybean after ultrasonic and enzymatic treatment were detected. The results showed that the combination of ultrasonic and enzymatic treatment could significantly reduce the antigenicity and immunological activity of β-conglycinin. The antigenic inhibition rate of-conglycinin decreased by 61.15% after 400 W and 15 min ultrasonic pretreatment of soybean protein by enzymatic treatment. SDS-PAGE results showed that ultrasonic combined with enzymatic treatment could break the protein peptide bond and change the linear epitope. Surface hydrophobicity results showed that the spatial structure of the protein was depolymerized and repolymerized, the third and fourth structures were destroyed, and conformational epitope was changed. The antigenic change of β-conglycinin is mainly due to the change of amino acid sequence and spatial structure of soybean protein caused by ultrasonic combined enzymatic hydrolysis.
分 类 号:TS201.2[轻工技术与工程—食品科学]
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