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Updated: Jan 20, 2026

Analyzing Large Protein Complexes by Structural Mass Spectrometry
Published on: June 19, 2010
熱処理時間変調ホエイタンパク質分離物-Lycium barbarum多糖類複合体における相互作用メカニズムの解明:構造機能進化の観点から
Shaomin Zheng1, Fangyan Huang1, Bingqiang Wang1
1College of Food and Bioengineering, Fujian Polytechnic Normal University, Fuqing, Fujian, China.
Abstract:
This study investigated the temporal evolution of the structure-function relationship in whey protein isolate-Lycium barbarum polysaccharide (WPI-LBP) complexes during 95 °C heating to identify optimal processing windows and underlying interaction mechanisms. The degree of grafting (DG) peaked at 60 min (37.43 %), confirmed electrophoretically. Solubility, emulsifying activity index (EAI), and thermal stability rose then fell with heating, while surface hydrophobicity (H0) and free sulfhydryl (SH) content were inversely correlated, with critical points at 30 and 60 min. Circular dichroism (CD) and X-ray diffractometer (XRD) analysis showed time-dependent changes in secondary and crystal structures. Microscopy revealed and water state analysis showed that moderate heating for 30 min produced complexes with smooth surfaces and uniform aggregates. Moreover, the results suggest that WPI-LBP complexes formation is primarily driven by covalent bonds and hydrophobic interactions, supplemented by hydrogen bonds and electrostatic forces. These findings offer theoretical guidance for utilizing WPI-LBP complexes in food applications.
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