Work

Formation and Structural Characteristics of Heating-Induced Amyloid Fibrils Derived from Rice Albumin at Different pH Values

Year: 2025

Type: article

Abstract: The comparison of rice albumin (RA) after heat treatment at neutral and acidic conditions was investigated in this study. Compared to the decreased thioflavin T (ThT) intensity of RA at pH 2 during heating, the ThT intensity of RA at pH 7 increased throughout the process of fibrillization. After fibrillization, the ThT intensity of RA at pH 7 was significantly increased by 27%, 38% and 35% at the protein concentrations of 1%, 2% and 4%, respectively. In addition, worm-like fibrils with a contour length of 100-300 nm were formed after heating at neutral conditions, accompanied by an increased average particle size and structural re-arrangement. Furthermore, the fibril formation at pH 7 involved the enhancement of an ordered β-sheet structure. However, only spherical agglomerate with a larger average particle size (>2000 nm) was observed when RA was heated at pH 2, because excessive hydrolysis destroyed the fibril-core sequences of RA. Additionally, the low solubility and high hydrophobicity of RA at pH 2 were not conducive to the formation of fibrils. In a word, a neutral environment is suitable for RA-based fibril formation, which provides a new insight for its future uses in food products.

Source: Foods

DOI: 10.3390/foods14173069

Authors: Ting Li, Li Wang

Institution: Jiangnan University

Language: English

Topic: Proteins in Food Systems

Subfield: Food Science

Field: Agricultural and Biological Sciences

Domain: Life Sciences

Open Access status: gold

Estimated APC paid: $3,499

Funders: Government of Jiangsu Province, Natural Science Foundation of Jiangsu Province, Fundamental Research Funds for the Central Universities