沙棘籽蛋白水解物的缬氨酸化:对形态、结构、功能和抗氧化性能的影响

JSFA reports Pub Date : 2023-04-17 DOI:10.1002/jsf2.113
Zakir Showkat Khan, Navdeep Singh Sodhi, Shemilah Fayaz, Rayees Ahmad Bakshi, Raashid Ahmad Siddiqi, Basharat N. Dar, Hari N. Mishra, Bhavnita Dhillon
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引用次数: 0

摘要

背景对营养缺乏、粮食安全和可持续性的日益关注强调了探索替代和可持续蛋白质来源的工作。在这项研究中,从沙棘籽中提取和利用蛋白质浓缩物和水解物,否则就是一种废物。使用各种酶,即胃蛋白酶(pH 2.0和37°C)、胰蛋白酶(pH 7.0和37°C)和鱼精蛋白(pH 7.0和50°C),不同的持续时间,即30、60、90和120 min对沙棘籽蛋白浓缩物(SSPC)的结构和功能特性进行了研究。结果胃蛋白酶水解的SSPC样品的乳化活性指数和溶解度显著高于胰蛋白酶和鱼精蛋白水解的SSPC样品。傅立叶变换红外研究表明,酶水解处理降低了酰胺I、II和III带的峰值强度。酶解后SSPC蛋白二级结构的β-折叠、β-转弯和无规卷曲发生了显著变化。粒径为295.8至440388至713.6399至890 胃蛋白酶、胰蛋白酶和鱼精蛋白分别为nm。胃蛋白酶处理样品的微观结构显示出比天然、胰蛋白酶和鱼精蛋白更多孔和松散的结构。经过不同时期的酶处理,所有样品的抗氧化活性都显著提高。结论富含蛋白质的水解产物为开发适用于各种食品配方的有效技术功能添加剂创造了新的机会。
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Valorization of sea buckthorn seed protein to hydrolysates: Impact on morphological, structural, functional, and antioxidant properties

Background

Increasing concerns about nutritional deficiency, food security, and sustainability have emphasized work on exploring alternative and sustainable sources of protein. In this study, an initiative to extract and utilize protein concentrates, and hydrolysates from sea buckthorn seed, otherwise a waste material, is undertaken. The effect of hydrolysis using various enzymes namely pepsin (pH 2.0 and 37°C), trypsin (pH 7.0 and 37°C), and protamex (pH 7.0 and 50°C), for different time durations, namely, 30, 60, 90, and 120 min, on the structural and functional properties of sea buckthorn seed protein concentrate (SSPC), was elucidated.

Results

The emulsifying activity index and solubility of pepsin-hydrolysed SSPC increased significantly and were higher than those of trypsin and protamex hydrolysed SSPC samples. A Fourier transformation infrared study revealed that the enzyme hydrolysis treatment reduced the peak intensity in amide I, II, and III bands. A significant change was found in the β-sheet, β-turn and random coiling of the secondary structure of SSPC protein by enzymatic hydrolysis. The particle size ranged from 295.8 to 440, 388 to 713.6, 399 to 890 nm for pepsin, trypsin, and protamex, respectively. The microstructure of pepsin-treated samples showed a more porous and loose structure than native, trypsin and protamex. Antioxidant activity increased significantly for all the samples with enzyme treatments carried out for different periods.

Conclusion

The results indicate that the protein-rich hydrolysates could create new opportunities for the development of effective techno-functional additives for use in a wide range of food formulations.

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