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Updated: May 24, 2025
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Structural characterization and emulsification properties of quinoa protein-dextran conjugates fabricated through
Jingzhao Feng1, Zhiyu Li2, Cuirong Luan2
1Fuzhou Institute of Oceanography, Minjiang University, Fuzhou 350108, China; Fujian Universities Key Laboratory of Molecular Plant-Microbe Interaction, Fujian Agriculture and Forestry University, Fuzhou 350002, China.
Abstract:
In this study, quinoa protein was grafted by dextran with varying molecular weights via the Maillard reaction, subjected to different ultrasound powers. Structural analysis revealed that dextran covalently bonded to the 11S globulin and B subunits of quinoa protein, causing the ordered structures transformed into β-turn and random coil. Among the conjugates, the one prepared with 40 kDa dextran at 200 W ultrasound power exhibited optimal modification effects, achieving a grafting degree of 28.6 %, a particle size of 91.01 nm, and a zeta potential of -39.3 mV. This conjugate had a low interfacial tension of 7.8 mN/m, attributed to its improved amphiphilic balance and enhanced steric stabilization. When applied to an oil-in-water system, the fabricated conjugate led to an emulsion with well-dispersed droplets and demonstrated excellent storage and creaming stability. Overall, this research advanced the functional utilization of quinoa protein, opening new avenues for its application as food material.
