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Updated: Aug 22, 2025
Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity
Published on: January 15, 2014
Analysis of the shape retention ability of antifreeze peptide-based surimi 3D structures: Potential in freezing and
Han Tian1, Xu Chen2, Congrong Chen2
1College of Chemical Engineering, Fuzhou University, Fuzhou 350108, PR China; College of Biological Science and Engineering, Fuzhou University, Fuzhou 350108, PR China.
Abstract:
The effects of freeze-thaw (F-T) cycles on the shape retention of antifreeze peptides-based surimi ink (ASI) 3D structures were analyzed. The results showed that the ASI 3D structure has good shape retention ability, and the width, height, weight, and water holding capacity were 22.42 mm, 21.07 mm, 9.99 g, and 68.30 % even after F-T 4 times, respectively. The average area and equivalent diameter of ice crystals in ASI 3D structures only expand from 0.001 mm2 and 0.040 mm to 0.015 mm2 and 0.139 mm, respectively. The α-helix and β-sheet of myofibrillar protein in ASI 3D structure were slightly decreased by 44.16 ± 0.98 % to 33.33 ± 0.92 % and increased by 18.28 ± 4.45 % to 24.43 ± 1.60 %, respectively. The chemical bond and protein interaction have changed to some extent. AFPs can prevent denaturation and juice loss of surimi 3D structures after F-T. The results provide theoretical guidance for maintaining the shape retention of frozen 3D food structures.
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