鱼类蛋白质化剂作为质地修改鱼产品中的蛋白质丰富剂
Leena Prabhu1, Aase Vorre Skuland1, Paula Varela1
1Nofima AS, Richard Johnsensgate 4, 4068 Stavanger, Norway.
Foods (Basel, Switzerland)
|January 25, 2025
概括
研究人员开发了一种新的碎和潮湿的鱼产品,用于食障碍患者. 这种质地修改的鱼符合国际消化不良饮食标准化倡议 (IDDSI) 5级,为长期储存提供了更好的质地和安全性.
科学领域:
- 食品科学 食品科学 食品科学
- 营养科学 营养科学
- 老年学是一门学科.
背景情况:
- 缺食症影响着数以百万计的人,需要专门的食物纹理.
- 质地修改的饮食,如碎和潮湿 (IDDSI 5 级),对于安全的吞至关重要.
- 鱼提供了高营养价值,但需要修改失消的饮食.
研究的目的:
- 开发一种适合食障碍患者的冷,质地修改的鱼产品.
- 为了实现国际消化障碍饮食标准化倡议 (IDDSI) 5级 (碎和潮湿) 标准.
- 为了确保吸引人的感官品质和安全的保质期.
主要方法:
- 大西洋鱼经过加工 (经过热处理,混合) 并用素,乳清蛋白和鱼蛋白水解剂重建.
- 产品经过热处理,冷却,并在4°C下储存29天.
- 分析包括微生物学,仪器纹理,感官评估和IDDSI叉压力测试.
主要成果:
- 与对照组相比,含有鱼蛋白水解剂的产品表现出增强的柔软性和降低的粘性.
- 感官分析证实了味道 (鱼味) 和质地 (柔软,粘性) 的显著差异,但没有苦味.
- 在冷藏保存29天后,微生物学分析证实了产品的安全性和质量.
结论:
- 一个冷却的,质地修改的鱼产品满足IDDSI 5级的成功开发.
- 该产品表现出良好的微生物质量,安全性和可期望的感觉/纹理特性.
- 这项创新支持老年护理设施和商业生产的功能障碍友好型食品.
相关概念视频
Protein Modifications in the RER
Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Protein Denaturation
The function of proteins depends on their native three-dimensional structure, which is dictated by the amino acid sequence of the specific protein. Folding of the polypeptide chain takes place under specific conditions that energetically favor the folded conformation. In contrast, protein denaturation occurs spontaneously under unfavorable conditions that disrupt the integrity of the folded conformation. Thus, the chemical and physical environment of a protein, such as significant changes in pH...


