超声辅助酶法脱酰胺处理开发用于吞咽困难的软质鱼糜凝胶:凝胶特性、体外消化率及蛋白质机制
Ultrasound-Assisted Enzymatic Deamidation Treatment for Developing Soft Surimi Gel for Dysphagia: Gel Properties, In Vitro Digestibility, and Protein Mechanisms.
文献信息
| PMID | 42737281 |
|---|---|
| 原文 | 在 PubMed 查看原文 ↗ |
| 发表日期 | 2026 |
| 作者 | Wei Wang |
| 作者单位 | National & Local Joint Engineering Research Center of Storage, Processing and Safety Control Technology for Fresh Agricultural and Aquatic Products, College of Food Science and Engineering, Bohai University, Jinzhou 121013, China. |
| 期刊 | Foods (Basel, Switzerland) |
| SCI 分区 | Q1 |
| IF | 6.5 |
| 研究类型 | 基础研究 · 基础/转化 |
| 所属专科 | 咽喉科 |
中文摘要
背景: 迫切需要开发满足吞咽困难患者需求的食物。方法:通过超声辅助蛋白质-谷氨酰胺酶(PG)脱酰胺处理制备了适合吞咽困难患者的软化鱼糜凝胶。结果:与对照组相比,添加0.2% PG的软化鱼糜凝胶的硬度和凝胶强度分别从607.40 g和530.79 g mm降至244.60 g和78.61 g mm,满足IDDSI 5级分类标准(p < 0.05)。PG的加入将鱼糜凝胶中的自由水转化为流动性较低的水,显著提高了凝胶的持水能力。超声辅助酶法脱酰胺处理使鱼糜凝胶在消化过程中产生更多小分子肽和游离氨基酸。该处理降低了肌原纤维蛋白凝胶中的疏水相互作用,增强了氢键,将α-螺旋结构提高至46.27%,并将β-折叠结构降低至19.18%,与对照组相比差异显著(p < 0.05)。色氨酸残基微环境的极性发生改变,阻碍了热诱导凝胶化过程中展开的蛋白质结构进一步折叠。结论:本研究为开发具有安全吞咽和营养特性的专用食品提供了基础理论框架。
英文摘要
An urgent necessity exists to create foods that cater to the requirements of patients with dysphagia. The softened surimi gel appropriate for dysphagia patients was produced through ultrasonic-assisted Protein-glutaminase (PG) deamidation treatment. In comparison to the control group, the hardness and gel strength of softened surimi gel with a 0.2% PG addition diminished from 607.40 g and 530.79 g mm to 244.60 g and 78.61 g mm, respectively, satisfying the IDDSI Level 5 classification criteria (p < 0.05). The incorporation of PG transformed free water in the fish paste gel into less mobile water, markedly improving the gel's water holding capacity. The ultrasound-assisted enzymatic deamidation treatment made the surimi gel produce more small molecular peptides and free amino acids during digestion. This treatment diminished hydrophobic interactions in myofibrillar protein gel, augmented hydrogen bonding, elevated the α-helix structure to 46.27%, and decreased the β-sheet structure to 19.18%, with significant differences compared to the control group (p < 0.05). The polarity of the tryptophan residue microenvironment alters and impeding the further folding of unfolded protein structures during heat-induced gelation. This study offers a fundamental theoretical framework for the development of specialized foods that possess safe swallowing and nutritional attributes.