Analysis of the shape retention ability of antifreeze peptide-based surimi 3D structures: Potential in freezing and thawing cycles. (30th March 2023)

• Record Type: Journal Article
• Authors: Tian, Han; Chen, Xu; Chen, Congrong; Wu, Jinhong; Huang, Jianlian; Zhao, Lei; Wang, Shaoyun
• Is Part Of: Food chemistry. Volume 405:Part A(2023)
• Publication Date: 2023-03-30
• Subjects: 3D structures -- Shape retention -- Antifreeze peptides -- Freeze-thaw cycles -- Ice crystal; Food -- Analysis -- Periodicals; Food -- Composition -- Periodicals; 664
• DOI: 10.1016/j.foodchem.2022.134780
• Languages: English
• ISSNs: 0308-8146

Abstract

Highlights: AFPs can reduce the shape retention deterioration of surimi 3D structure after F-T. SEM was used to characterize the size of ice crystals of 3D structure. Protein interactions were illustrated by a weak gel model and chemical bonds. CD and DSC were used to characterize secondary structure and degree of denaturation. 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 mm 2 and 0.040 mm to 0.015 mm 2 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.