数字农科院2.0

Modulating interfacial structure and lipid digestion of natural Camellia oil body by roasting and boiling processes

文献类型: 外文期刊

作者: Chen C.; Pan Y.; Niu Y.; Peng D.; Huang W.; Shen W.; Jin W.; Huang Q.

作者机构:

关键词: Calcination; Cell proliferation; Electrophoresis; Hydrophobicity; Oilseeds; Phospholipids; Proteins; Stability; Body surface; Confocal Raman; Interfacial composition; Interfacial structures; Lipid digestions; Oil bodies; Physical stability; Roasting process; Structure stability; Surface hydrophobicity; Zeta potential; fat droplet; linoleic acid; lipid; oleic acid; phenylalanine; phospholipid; plant protein; tocopherol; tryptophan; vegetable oil; adsorption; Article; boiling (food); Camellia; Camellia oleifera; chemical structure; confocal laser scanning microscopy; controlled study; differential scanning calorimetry; digestion; glycation; heating; hydrophobicity; in vitro study; intestine fluid; ionic strength; oil body; oilseed; particle size; pH; plant seed; polyacrylamide gel electrophoresis; protein analysis; protein denaturation; protein depletion; protein structure; Raman spectrometry; roasting; surface charge; surface property; thermostability; transmission electron microscopy

期刊名称: Food Chemistry

ISSN: 0308-8146

年卷期: 2023 年 402 卷

页码:

收录情况: SCIE(2023版) ; ; EI(2023版)

摘要: Oil body (OB) is the lipid-storage organelle in oilseed, and its stability is crucial for oilseed processing. Herein, effects of roasting and boiling on the structure, stability, and in vitro lipid digestion of Camellia OB were studied. The interfacial structure and physical stability of the extracted OB were investigated by electrophoresis, confocal-Raman spectroscopy, zeta-potential, and surface hydrophobicity, etc. Boiling caused protein loss on the OB surfaces, forming a stable phospholipid interface, which resulted in coalescence of the droplets (d > 100 μm) and negative ζ-potential (-3 ∼ -8 mV) values at a pH of 2.0. However, roasting partially denatured the proteins in the seeds, which were adsorbed on the OB surfaces. The random coil structure of interfacial protein increased to ∼20 % after thermal treatment. Besides, heating decreased the surface hydrophobicity of OB and improved lipid digestion. After boiling 60 min, the extent of lipolysis increased from 41.7 % (raw) to 57.4 %. © 2022 Elsevier Ltd

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