Mechanism Unraveling the Ice-Inhibition Differences of Inulin with Varied Polymerization Degrees and Its
Shichen Zhu1, Ningning Peng1, Rongrong Mu1
1Key Laboratory of Green, Low-Carbon and Efficient Development of Marine Fishery Resources, National R&D Branch Center for Pelagic Aquatic Products Processing (Hangzhou), College of Food Science and Technology, Zhejiang University of Technology, Hangzhou 310014, Zhejiang, China.
Abstract:
In this work, the ice-inhibiting effects and their underlying mechanisms of inulin with various chain lengths were elucidated through experimental measurements and molecular dynamics simulations. The results suggested that long-chain inulin (HP group) exhibited strong and stable ice-inhibiting effects, with a minimum %MGS (12.18%) and limited ice growth of 36.61% after 100 min of freezing. The extensive contact area of long-chain inulin with water molecules (higher Rg and solvent-accessible surface area (SASA) values) favored their hydrogen-bond formation, which further disrupted the original hydrogen-bonding network of water by transforming the hydrogen-bonding mode (DDAA-OH mode into the DA mode). The remarkable cryoprotective effects of the HP group on scallops were evidenced by no significant difference in mass loss, water-holding capacity (WHC), and structural stability of the myofibrillar protein with the commercial antifreeze group (p > 0.05). This study provides strong evidence to broaden the cryoprotection applications of inulin to improve the quality of frozen food.
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