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Updated: Aug 24, 2026

Improved In-gel Reductive β-Elimination for Comprehensive O-linked and Sulfo-glycomics by Mass Spectrometry
Published on: November 20, 2014
Unravelling the digestion differences in ovalbumin gels modulated by varying saccharide chain length
Min Huang1, Jingjing Shang2, Qing Cao2
1School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China; Key Laboratory for Food Microbial Technology of Zhejiang Province, School of Food Science and Biotechnology, Zhejiang Gongshang University, Hangzhou 310018, China.
Abstract:
The influence of varying protein-saccharide interaction strength on the gelation properties of ovalbumin (OVA) gels was investigated using ι-Carrageenan (ι-CG) and ι-carrageenan oligosaccharides (ι-CO) as representative saccharides. Addition of both saccharides inhibited the thermal aggregation of OVA. OVA/ι-CO gels showed a lower complex modulus (G*) during gelation. Incorporating either ι-CG or ι-CO reduced the apparent viscosity, storage and loss moduli (G' and G"), hardness, and water holding capacity of the complex gels. The degradation temperature increased in OVA/ι-CG gels (332.5 °C) but decreased in OVA/ι-CO gels (317.2 °C) compared to pure OVA gels (322.8 °C). Unfolded ι-CG chains induced highly porous and irregular gel networks. Furthermore, in vitro simulated gastrointestinal digestion showed that both saccharides reduced overall protein digestibility. Specifically, at a saccharide concentration of 0.10%, gastric digestibility decreased from 26.43% to 22.32% (OVA/ι-CG) and 24.69% (OVA/ι-CO), while intestinal digestibility decreased from 80.25% to 73.65% (OVA/ι-CG) and 76.09% (OVA/ι-CO). These findings offer mechanistic insights for designing novel bio-based egg protein gels with desired texture and controlled digestive properties.
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