中国农业科学院农业信息研究所 中国农学会
Agricultural Information Institute of CAAS China Association of Agricultural Science Societies
En
Ch
中国农业科学院农业信息研究所 中国农学会 主办

AI检索

订阅

返回顶部
当前位置: 首页 > 文章 > 超高压结合胰蛋白酶消减虾原肌球蛋白致敏性及其抗原线性表位残留 食品科学 2019 (21) 107-114
Position: Home > Articles > Allergenicity Reduction of Shrimp Tropomyosin by High Hydrostatic Pressure Treatment Combined with Enzymatic Hydrolysis and Its Linear Epitope Residues FOOD SCIENCE 2019 (21) 107-114

超高压结合胰蛋白酶消减虾原肌球蛋白致敏性及其抗原线性表位残留

作  者：
胡志和;王丽娟;薛璐;刘平;贾莹;鲁丁强
单  位：
天津商业大学生物技术与食品科学学院天津市食品生物技术重点实验室
关键词：
原肌球蛋白;超高静压;胰蛋白酶;致敏性;线性表位
摘  要：
比较常压下酶水解与超高压下酶水解虾原肌球蛋白(tropomyosin,TM)的致敏性差异及线性表位的残留,探讨超高压下酶水解TM增强致敏性消减效果的原因。采用间接酶联免疫吸附测定法检测TM致敏性,傅里叶变换红外光谱和荧光光谱法检测TM二级和三级结构;以致敏性(OD_(492 nm))为指标,确定常压和超高压下酶水解TM的条件;采用质谱法检测水解片段的氨基酸序列。结果表明,在40℃、200 MPa下,保压时间30 min有利于胰蛋白酶活力的提高;压力在100～600 MPa内,TM致敏性随压力升高而降低,其致敏性与二级结构中β-转角的相对含量及三级结构的变化有关;在常压下(40℃、酶添加量3 000 U/g、水解30 min),TM水解产物的致敏性消减率为89%,水解产物中含8～16个氨基酸残基的片段数量占76.8%,且线性表位的消减率为60.0%～66.7%;在超高压下(40℃、酶添加量3 000 U/g、200 MPa下水解30 min),TM水解产物的致敏性消减率为98%,水解产物中含8～16个氨基酸残基的片段数量占93.3%,且线性表位的消减率为88.9%～90.0%。因此,超高压可以促进酶水解TM,有利于线性表位的消除,从而降低水解产物的致敏性。
译  名：
Allergenicity Reduction of Shrimp Tropomyosin by High Hydrostatic Pressure Treatment Combined with Enzymatic Hydrolysis and Its Linear Epitope Residues
作  者：
HU Zhihe;WANG Lijuan;XUE Lu;LIU Ping;JIA Ying;LU Dingqiang;Tianjin Key Laboratory of Food Biotechnology, School of Biotechnology and Food Science,Tianjin University of Commerce;
关键词：
tropomyosin;;high hydrostatic pressure;;trypsin;;allergenicity;;linear epitope
摘  要：
The objective of this work was to compare the differences in the allergenicity and linear epitope residues of trypsin hydrolysates of tropomyosin(TM) prepared under normal and high pressure conditions and to discuss the reason why allergenicity reduction of hydrolyzed TM is enhanced under high pressure. The allergenicity was detected by indirect enzyme-linked immunosorbent assay(iELISA), and the secondary and tertiary structures were investigated by infrared and fluorescence spectroscopies. Optimal hydrolysis conditions under normal and high pressure were determined based on the binding capacity of hydrolysate to antibody(OD_(492 nm)). Mass spectrometry(MS) was used for detecting the amino acid sequences of hydrolytic fragments. The results showed that trypsin activity was enhanced after treatment for 30 min under 200 MPa at 40 ℃. The allergenicity of high-pressure treated TM decreased with increasing pressure from 100 to 600 MPa, and it was related to changes in the relative content of β-turn structure and in tertiary structure. The allergenicity of TM was reduced by 89% and 98% after 30 min hydrolysis with 3 000 U/g of trypsin at 40 ℃ under normal pressure and 200 MPa, respectively. The percentage of fragments containing 8–16 amino acid residues in the hydrolysates was 76.8% and 93.3%, respectively, and the linear epitopes were reduced by 60.0%–66.7% and 88.9%–90.0%, respectively. Therefore, high pressure treatment could promote the enzymatic hydrolysis of TM, facilitating the elimination of linear epitopes and reducing the allergenicity of hydrolyzed products.

相似文章

导出引用
计量
文章访问数: 12
HTML全文浏览量: 0
PDF下载量: 0

所属期刊

推荐期刊

友情链接Friendly link
农业信息研究所Agricultural information institute 农业智能知识服务平台Agricultural intelligent knowledge service platform 农业学术服务平台Agricultural Knowledge Service System 中国知网CNKI 维普网VIP 万方WANFANG DATA
联系我们Contact us

电话Tell：010-82109652-808

邮箱E-mail：agrijournal@caas.cn

服务Service
关于我们About us 意见建议Opinions and suggest
版权说明Copyright
单位：中国农业科学院农业信息研究所 中国农学会 © 2017中国农业科学院农业信息研究所 ICP备案号：京ICP备09089781号-46