Effects of chemical modifications on allergenicity and functional properties of silkworm pupae proteins

IF 9.8 1区 农林科学 Q1 CHEMISTRY, APPLIED
Songyuan Huang , Xue Feng , Wenqi Yue , Philippe Madjirebaye , Xuchao Deng , Yuting Fan , Jiamin Chen , Xuli Wu
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引用次数: 0

Abstract

Silkworm pupae proteins (SPP) have been exploited as a new functional protein, but there are still some people who are allergic to it. This study investigated the effects of different chemical modifications (phosphorylation, succinylation, deamidation, glycosylation) on SPP's allergenicity and its structural and functional impact. Spectroscopic analysis showed that all three modifications except glycosylation loosened the three-dimensional structure of SPP. Enzymatic hydrolysis studies have shown that the succinylated group can significantly enhance the hydrolysis resistance of SPP at 30 kDa, and the ability to bind IgE was maintained. Most proteins were hydrolyzed into small peptides within 30 min after combined digestion. A functional study of chemically modified SPP demonstrated that succinylation had a strong water-holding capacity. Further deamidation and phosphorylation have stupendous foaming ability and foaming stability, respectively. This discovery collectively will provide the experimental basis for developing and using silkworm pupae protein in the food industry.
化学修饰对家蚕蛹蛋白致敏性和功能特性的影响
蚕蛹蛋白(SPP)作为一种新的功能蛋白已被开发出来,但仍有一些人对其过敏。本研究考察了不同化学修饰(磷酸化、琥珀酰化、脱酰胺化、糖基化)对SPP致敏性的影响及其结构和功能的影响。光谱分析表明,除糖基化外,三种修饰均使SPP的三维结构松动。酶解研究表明,琥珀基化基团能显著增强SPP在30 kDa下的抗水解能力,并保持其结合IgE的能力。大多数蛋白质在30 min内水解成小肽。化学修饰SPP的功能研究表明琥珀酰化具有很强的持水能力。进一步脱酰胺和磷酸化分别具有惊人的发泡能力和发泡稳定性。这一发现将为蚕蛹蛋白在食品工业中的开发和利用提供实验依据。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
Food Chemistry
Food Chemistry 工程技术-食品科技
CiteScore
16.30
自引率
10.20%
发文量
3130
审稿时长
122 days
期刊介绍: Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.
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