| 夏易玄1， 朱玲1， 刘通通2， 吴港城1， 齐希光1， 王立1， 钱海峰1， 张晖1.热处理和高速剪切对豌豆蛋白水解效率及其水解物性质的影响[J].中国油脂,2023,48(3):.[XIA Yixuan1, ZHU Ling1, LIU Tongtong2, WU Gangcheng1, QI Xiguang1,WANG Li1, QIAN Haifeng1, ZHANG Hui1.Effect of heat treatment and high-speed shear on the hydrolysis efficiency of pea protein and the properties of its hydrolysates[J].China Oils and Fats,2023,48(3):.] |
| 热处理和高速剪切对豌豆蛋白水解效率及其水解物性质的影响 |
| Effect of heat treatment and high-speed shear on the hydrolysis efficiency of pea protein and the properties of its hydrolysates |
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| DOI： |
| 中文关键词: 豌豆蛋白 热处理 高速剪切 水解效率 蛋白水解物 |
| 英文关键词:pea protein heat treatment high-speed shear hydrolysis efficiency protein hydrolysates |
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| 中文摘要: |
| 为提高豌豆蛋白的酶水解敏感性及其水解物的抗氧化活性，分别考察95℃、10 min的热处理和10 000×g、10 min的高速剪切对豌豆蛋白水解性能的影响并探究其改善原因。结果表明，热处理和高速剪切均提高了豌豆蛋白的水解度、氮回收率以及水解物的抗氧化活性（p<0.05），高速剪切提高了不溶性聚集体比例，而热处理使其降低，其中热处理优化效果更为明显，水解度和氮回收率分别增加了21.1%和9.6%，不溶性聚集体降低了27.7%。热处理和高速剪切使豌豆蛋白溶解度显著提高，使豌豆蛋白水解物氨基酸含量和小分子肽比例显著增加（p<0.05）。采用红外光谱和扫描电子显微镜观察预处理前后豌豆蛋白的二级结构和表观形貌的变化发现，两种预处理方式在不同程度上促使了豌豆蛋白紧密结构的展开，有助于实现豌豆蛋白的高效水解。综上，热处理相对于高速剪切更有利于提高豌豆蛋白的水解效率。 |
| 英文摘要: |
| To improve the enzymatic hydrolysis sensitivity of pea protein and antioxidant activity of pea protein hydrolysates, the effects of heat treatment at 95℃ for 10 min and high-speed shear at 10 000×g for 10 min on the hydrolysis performance of pea protein were investigated and the reasons for their improvement were investigated. The results showed that both heat treatment and high-speed shear improved the hydrolysis degree, nitrogen recovery, and antioxidant activity of pea protein after enzymolysis (p<0.05). High-speed shear improved the proportion of insoluble aggregates, while heat treatment did the opposite. The improvement effect of heat treatment was more obvious, the hydrolysis degree increased by 21.1%, the nitrogen recovery increased by 9.6%, and the proportion of insoluble aggregates decreased by 27.7%. The heat treatment and high-speed shear increased significantly solubility of pea protein and increased obviously the amino acid content and the proportion of small-molecule peptides in the pea protein hydrolysate (p<0.05). The changes in secondary structure and apparent morphology of pea protein before and after hydrolysis found by infrared spectroscopy and scanning electron microscopy suggested that the two pretreatments contributed to the unfolding of the compact structure of pea protein to different degrees and helped to achieve efficient hydrolysis of pea protein. In conclusion, heat treatment is more favourable than high-speed shear to improve the hydrolysis efficiency of pea protein. |
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