Huang Songyuan, Feng Xue, Yue Wenqi, Madjirebaye Philippe, Deng Xuchao, Fan Yuting, Chen Jiamin, Wu Xuli
Medical School of Pharmaceutical Sciences, Health Science Center, Shenzhen University, Shenzhen 518060, Guangdong Province, PR China.
School of Public Health, Health Science Center, Shenzhen University, Shenzhen 518060, Guangdong Province, PR China.
Food Chem. 2025 Jun 15;477:143635. doi: 10.1016/j.foodchem.2025.143635. Epub 2025 Feb 27.
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.
蚕蛹蛋白(SPP)已被开发为一种新型功能蛋白,但仍有一些人对其过敏。本研究调查了不同化学修饰(磷酸化、琥珀酰化、脱酰胺化、糖基化)对SPP致敏性及其结构和功能的影响。光谱分析表明,除糖基化外,其他三种修饰均使SPP的三维结构松弛。酶解研究表明,琥珀酰化基团可显著提高SPP在30 kDa时的抗水解能力,并保持其结合IgE的能力。联合消化后,大多数蛋白质在30分钟内被水解成小肽。对化学修饰的SPP进行的功能研究表明,琥珀酰化具有很强的持水能力。进一步的脱酰胺化和磷酸化分别具有巨大的发泡能力和发泡稳定性。这一发现将共同为蚕蛹蛋白在食品工业中的开发和应用提供实验依据。