Investigation on the quality regulating mechanism of antifreeze peptides on frozen surimi: From macro to micro

[Display omitted] •Antifreeze peptides from Takifugu obscurus skin (TsAFP) inhibit ice recrystallization.•4% TsAFP can cryoprotect surimi from deterioration caused by ice crystals.•TsAFP can significantly inhibit the freeze denaturation and oxidation of proteins.•TsAFP binds to myosin cavity to reta...

Full description

Saved in:
Bibliographic Details
Published in:Food research international 2023-01, Vol.163, p.112299-112299, Article 112299
Main Authors: Yang, Fujia, Jiang, Wenting, Chen, Xu, Wu, Jinhong, Huang, Jianlian, Cai, Xixi, Wang, Shaoyun
Format: Article
Language:English
Subjects:
Antifreeze peptides
Antifreeze Proteins
Cryoprotectant
Cryoprotective Agents - chemistry
Cryoprotective Agents - pharmacology
Freezing
Ice
Molecular docking
Myofibrillar protein
Myosins
Protective mechanism
Surimi
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:[Display omitted] •Antifreeze peptides from Takifugu obscurus skin (TsAFP) inhibit ice recrystallization.•4% TsAFP can cryoprotect surimi from deterioration caused by ice crystals.•TsAFP can significantly inhibit the freeze denaturation and oxidation of proteins.•TsAFP binds to myosin cavity to retain protein structure and water holding ability.•TsAFP can be provided as an efficient cryoprotectant for frozen surimi. Freeze denaturation of protein caused by ice crystals is the main motivation for the quality deterioration of surimi during circulation and storage. This investigation aimed to cryoprotect surimi by adding antifreeze peptides from Takifugu obscurus skin (TsAFP) which can inhibit ice recrystallization, and to elucidate regulating mechanism. The comprehensive results showed that 4% TsAFP, half dosage of commercial cryoprotectant, had good cryoprotection on surimi by reducing the moisture variation and maintaining protein solubility of surimi at macro level, as well as inhibiting the degeneration and structure changes of myofibrillar proteins at micro level. Meanwhile, TsAFP could directly bind to the structural cavity of myosin, inhibit protein freezing-induced oxidation, maintain the spatial structure of myosin and water retention ability to preserve the surimi quality. This study helped better comprehend the protective mechanisms of antifreeze peptides in frozen surimi and was expected to provide a promising cryoprotectant for low-sweetness and low-calorie surimi.
ISSN:0963-9969
1873-7145
DOI:10.1016/j.foodres.2022.112299