豆蛋白分离物和银鱼蛋白的复合凝的凝特性和结构特征
Li Zheng1,2, Joe M Regenstein3, Linyi Zhou4
1College of Food Science, Northeast Agricultural University, Harbin 150030, China.
Gels (Basel, Switzerland)
|May 26, 2023
概括
改性大豆蛋白分离物 (SPI) 通过改善纹理和保持水分的能力来提高银鱼蛋白 (SCP) 凝质量. 对SPI的Papain处理产生了一种复合凝,其结构完整性得到改善,鱼味减少.
科学领域:
- 食品科学 食品科学 食品科学
- 蛋白质化学 蛋白质化学
- 生物技术是生物技术.
背景情况:
- 银鱼蛋白 (SCP) 患有凝质量差,包括不良气味和低凝强度.
- 提高基于SCP的产品的质地和稳定性对于扩大其利用是至关重要的.
研究的目的:
- 通过加入改性大豆蛋白分离物 (SPI) 来增强银鱼蛋白 (SCP) 的凝质量.
- 调查帕帕因受限水解对SPI的影响及其随后对SCP凝特性的影响.
主要方法:
- 豆蛋白分离物 (SPI) 用帕帕因进行治疗,以诱导受限制的水解,增加β-sheet结构.
- 经过修改的SPI与SCP使用谷氨酸转胺酶 (TG) 交叉连接,以形成复合凝.
- 凝的特性 (硬度,弹性,凝聚力,水能力) 和结构特征使用各种技术进行了分析,包括SEM.
主要成果:
- 修改后的SPI显著提高了SCP凝的硬度,弹性,性,凝聚性和保持水分的能力 (p < 0.05).
- 对于SPI,在0.5%的水解度 (DH) 实现了最佳结果.
- 帕帕因修饰增加了和二硫化物键,导致通过SEM观察到更复杂和更均的凝结构.
- 过度的水解对TG交联产生了负面影响.
结论:
- 修改了Papain的SPI有效地改善了银鱼蛋白质的凝纹理和保持水分的能力.
- 对SPI的受控酶化水解是成功的TG介导交联和复合凝形成的关键.
- 修改后的SPI提供了一个有前途的策略,以提高白银鱼蛋白质产品的质量和价值.
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