纤维
淀粉样纤维
淀粉样蛋白(真菌学)
面筋
化学
机制(生物学)
表征(材料科学)
蛋白质折叠
生物化学
小麦面筋
生物物理学
谷氨酰胺
氨基酸
纳米技术
淀粉样β
材料科学
生物
医学
病理
疾病
无机化学
哲学
认识论
作者
Huijuan Zhang,Shihao Lv,Chengming Jin,Feiyue Ren,Jing Wang
标识
DOI:10.1016/j.ijbiomac.2023.126435
摘要
Amyloid fibrils have excellent structural characteristics, such as a high aspect ratio, excellent stiffness, and a wide availability of functional groups on the surface. More studies are now focusing on the formation of amyloid fibrils using food proteins. Protein fibrillation is now becoming recognized as a promising strategy for enhancing the function of food proteins and expanding their range of applications. Wheat gluten is rich in glutamine (Q), hydrophobic amino acids, and the α-helix structure with high β-sheet tendency. These characteristics make it very easy for wheat gluten to form amyloid fibrils. The conditions, formation mechanism, characterization methods, and application of amyloid fibrils formed by wheat gluten are summarized in this review. Further exploration of amyloid fibrils formed by wheat gluten will reveal how they can play a significant role in food, biology, and other fields, especially in medicine.
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