Exploring the potential of enzymatic hydrolysis combined with glycosylation to modify soy glycinin: Insights into conformational flexibility, interfacial and emulsifying behavior

This research aimed to improve the conformational flexibility, oil/water interface and emulsifying properties of soy glycinin (11S) by enzymatic hydrolysis and glycosylation with carboxymethyl cellulose (CMC, 0–0.75 %, w/v). Enzymatic hydrolysis increased degree of grafting of 11S to CMC, with a maximum observed at 0.5 % CMC concentration. SR-FTIR tracing showed that 11S-CMC reacted mainly by inducing C O, C O and O H changes, while hydrolysis enhanced the C N effect. Pepsin hydrolysis disrupted disulfide bonds in 11S and increased protein flexibility; CMC enhanced steric hindrance through covalent grafting. The synergistic modification promoted interfacial diffusion, penetration and rearrangement of 11S to form more stable interfacial film. The modified protein-stabilized emulsions showed reduced droplet size and more uniform distribution, increased emulsifying activity and stability to 54.52 m 2 /g and 105.52 min. Rheological data displayed elevated apparent viscosity, G′, G″ and LAOS response properties of emulsions. These findings offer a dual-modification approach to enhance emulsifying potential of 11S.