蛋白质去化是否增强了大米蛋白缩物产生和稳定高内部相乳液的能力?
Danilo C Vidotto1, Andrêssa Maria Medeiros Theóphilo Galvão1, Guilherme M Tavares2
1Departamento de Engenharia e Tecnologia de Alimentos, Faculdade de Engenharia de Alimentos, Universidade Estadual de Campinas (UNICAMP), Campinas, Brazil.
Food research international (Ottawa, Ont.)
|February 11, 2024
概括
性除化改善了蛋白缩物 (RPC) 的溶解性,使得稳定的高内部相乳液 (HIPEs) 能够产生. 整个蛋白质分量 (DT) 对HIPE生产显示出有前途的结果,具有作为脂肪替代物的潜力.
科学领域:
- 食品科学与技术 食品科学与技术
- 蛋白质化学 蛋白质化学
- 合体和表面科学科学
背景情况:
- 米蛋白缩剂 (RPC) 是一种营养丰富,低过敏的蛋白质来源,含量高的素.
- 原生RPC的低溶解度限制了其在食品工业中的应用.
- 性除化是一种增强蛋白质功能的一种潜在方法.
研究的目的:
- 通过性除化,提高蛋白缩物 (RPC) 的可溶性和功能性质.
- 评估改性大米蛋白分量的形成和稳定高内部相乳液 (HIPEs) 的潜力.
- 评估HIPEs作为潜在的脂肪替代品的稳定性和质性质.
主要方法:
- 米蛋白缩物 (RPC) 经过性脱化 (343K,pH 11,0.5小时).
- 分离了两种蛋白质分离物:全脱胺蛋白 (DT) 和可溶性脱胺蛋白 (DS).
- 蛋白质分散的特征是 (溶解性,疏水性,泽塔潜力);HIPEs是用油形成的,并分析了60天的稳定性 (油,油损失) 和风湿性.
主要成果:
- 脱化显著增加了RPC的溶解性,使HIPE能够在75%的甘油中形成.
- 用DT和DS分散形成的HIPEs表现出高稳定性 (,低油损) 和良好的质恢复.
- 用DT分散生成的HIPE在60天内显示出更好的结构完整性,并且更具成本效益.
结论:
- 性除化有效地提高了用于食品应用的米蛋白功能.
- 修改后的米蛋白,特别是DT分数,可以成功地创建稳定的高内相乳液.
- 这些HIPE显示出作为食品中的脂肪替代品的巨大潜力.
相关概念视频
Protein Denaturation
4.2K
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...
4.2K
Protein Folding
8.0K
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
8.0K
Protein Folding Quality Check in the RER
3.7K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
3.7K


