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Updated: May 23, 2026
Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders
Published on: April 14, 2015
Multispectral analysis and molecular simulation of interaction mechanism between charged polysaccharides and
Jian Shi1, Naiyong Xiao2, Mingyu Yin2
1State Key Laboratory of Marine Food Processing & Safety Control, College of Food Science and Engineering, Ocean University of China, Qingdao 266003, China; College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.
Abstract:
Aquatic proteins exhibit poor stability and loose spatial structures, resulting in suboptimal functional characteristics. The present study investigates the interaction mechanism of various charged polysaccharides (quaternary chitosan (QCS), locust bean gum (LBG), and pectin (PT)) with myofibrillar protein in grass carp (MP) and conformation variations of complex particles, thus affecting the functional properties. The endogenous fluorescence of protein can be quenched by polysaccharides and the quenching rate is higher for positively charged polysaccharides. Moreover, the binding site of polysaccharide-myofibrillar protein interactions followed the order of QCS > PT > LBG. The molecular simulation results suggested that these polysaccharides enhance MP structural stability primarily through electrostatic and hydrogen-bonding interactions. Consequently, various charged polysaccharides resulted in a more stable structure, which conferred better emulsification and foaming properties to complexes. This study provides fundamental insights into charge-driven biopolymer interactions and scientific rationale for novel emulsifier and crosslinking agent of future food.
