Modulating the in vitro gastric digestion of heat-induced beta-lactoglobulin aggregates: Incorporation with polysaccharide

• Published in: Food chemistry Vol. 354; p. 129506
• Main Authors: Ma, Ruixiang, Lin, Zhantuo, Wu, Yuehan, Gao, Zhiming, Hu, Bing, Xu, Longquan, Fang, Yapeng, Nishinari, Katsuyoshi
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 30.08.2021
• Subjects: Dextran Sulfate - chemistry; Digestion; Digestion behavior; Dithiothreitol - chemistry; Heat-induced protein aggregates; Hot Temperature; Hydrogen-Ion Concentration; Hydrophobic and Hydrophilic Interactions; Lactoglobulins - chemistry; Protein Aggregates; Protein fibril aggregates; Protein nanoparticles; Protein-polysaccharide interaction; Sodium Dodecyl Sulfate - chemistry; Protein fibril aggregates; Digestion behavior; Protein nanoparticles; Protein-polysaccharide interaction; Heat-induced protein aggregates
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2021.129506

[Display omitted] •Three protein aggregates were comparatively analyzed on their digestion behavior.•Effect of surface hydrophobicity and disulfide bond on the digestion were analyzed.•Digestion degree of the protein aggregates could be modulated by polysaccharides.•Surface hydrophobicity had much stronger effects than disulfide bond content. Three heat-induced protein aggregates, beta-lactoglobulin fibrils (BLGF), nanoparticles (BLGN), and worm-like aggregates (BLGW) were chosen to probe the effect of disulfide bond and surface hydrophobicity on their gastric digestion behavior. Furthermore, the effect of polysaccharide (dextran sulfate sodium, DSS) on the digestion behavior of the protein aggregates was investigated. Results showed that disulfide bond had a mild restraint on the digestion extent (maximum up to 4.65%), especially when its content was below 1 mol/mol, while the surface hydrophobicity had a stronger influence (up to 8.96%), and there is definitive positive linear relationship between the surface hydrophobicity and the digestion extent. When incorporated with DSS, both the disulfide bond content and surface hydrophobicity of the aggregates decreased, consequently, and the digestion was impeded, confirming the stronger effect from the surface hydrophobicity. The digestion extent of the heat-induced protein aggregates could be modulated linearly by incorporation of polysaccharide.