Investigation of the cryoprotective mechanism and effect on quality characteristics of surimi during freezing storage by antifreeze peptides

被引：73
作者：
Chen, Xu [1 ,2 ,3 ]
Wu, Jinhong [4 ]
Li, Xiaozhen [2 ]
Yang, Fujia [2 ]
Yu, Luhan [2 ]
Li, Xiaokun [2 ]
Huang, Jianlian [1 ,3 ]
Wang, Shaoyun [2 ]
机构：
[1] Minist Agr & Rural Affairs, Key Lab Refrigerat & Conditioning Aquat Prod Proc, Xiamen 361022, Peoples R China
[2] Fuzhou Univ, Coll Biol Sci & Engn, Fuzhou 350108, Fujian, Peoples R China
[3] Fujian Anjoy Foods Co Ltd, Xiamen 361022, Peoples R China
[4] Shanghai Jiao Tong Univ, Sch Agr & Biol, Dept Food Sci & Engn, Shanghai 200240, Peoples R China
来源：
FOOD CHEMISTRY | 2022年 / 371卷
基金：
国家重点研发计划;
关键词：
Frozen storage; Surimi; Recrystallization; Antifreeze peptides; Cryoprotective mechanism; ICE-BINDING PROTEINS; FROZEN STORAGE; PIGSKIN COLLAGEN; MUSCLE PROTEINS; TREHALOSE; DOUGH; MEAT;
D O I：
10.1016/j.foodchem.2021.131054
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
Freezing technology is important for storage of animal products such as surimi. However, mechanical damage caused by ice crystals would lead to quality deterioration. This study aims to investigate the protective effect of antifreeze peptides (AFPs) on the quality of surimi during freezing storage and its possible mechanism. We found that AFPs exhibited a strong inhibition of ice crystal recrystallization, and the molecular weight ranged from 180 to 3000 Da. AFPs can prevent the degeneration of myofibrillar protein by reducing the loss of Ca2+-ATPase activity, slowing oxidation of sulfhydryl groups to disulfide bonds, and maintaining surface hydrophobicity and solubility of myofibrillar protein. Moreover, AFPs can reduce the influence of freezing stress on water mobility, thereby protecting the surimi from losing immobilized water and bound water during frozen storage. These findings indicate that AFPs could potentially serve as a food ingredient with antifreeze functional for the storage of surimi products.
引用
收藏
页数：9
相关论文
共 34 条
  • [1] Superchilling of muscle foods: Potential alternative for chilling and freezing
    Banerjee, Rituparna
    Maheswarappa, Naveena Basappa
    [J]. CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION, 2019, 59 (08) : 1256 - 1263
  • [2] Ice-Binding Proteins and Their Function
    Bar Dolev, Maya
    Braslavsky, Ido
    Davies, Peter L.
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, VOL 85, 2016, 85 : 515 - 542
  • [3] Two-dimensional surface display of functional groups on a β-helical antifreeze protein scaffold
    Bar, Maya
    Scherf, Tali
    Fass, Deborah
    [J]. PROTEIN ENGINEERING DESIGN & SELECTION, 2008, 21 (02) : 107 - 114
  • [4] Physicochemical changes in Pacific whiting muscle proteins during iced storage
    Benjakul, S
    Seymour, TA
    Morrissey, MT
    An, HJ
    [J]. JOURNAL OF FOOD SCIENCE, 1997, 62 (04) : 729 - 733
  • [5] Benjakul S, 2000, J SCI FOOD AGR, V80, P1143, DOI 10.1002/1097-0010(200006)80:8<1143::AID-JSFA610>3.0.CO
  • [6] 2-C
  • [7] Modulating the aggregation of myofibrillar protein to alleviate the textural deterioration of protein gels at high temperature: The effect of hydrophobic interactions
    Chen, Bo
    Guo, Jie
    Xie, Yong
    Zhou, Kai
    Li, Peijun
    Xu, Baocai
    [J]. FOOD CHEMISTRY, 2021, 341
  • [8] Production, structure-function relationships, mechanisms, and applications of antifreeze peptides
    Chen, Xu
    Wu, Jinhong
    Cai, Xixi
    Wang, Shaoyun
    [J]. COMPREHENSIVE REVIEWS IN FOOD SCIENCE AND FOOD SAFETY, 2021, 20 (01) : 542 - 562
  • [9] Ice-binding proteins: a remarkable ice crystal regulator for frozen foods
    Chen, Xu
    Shi, Xiaodan
    Cai, Xixi
    Yang, Fujia
    Li, Ling
    Wu, Jinhong
    Wang, Shaoyun
    [J]. CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION, 2021, 61 (20) : 3436 - 3449
  • [10] Effects of gelatin-based antifreeze peptides on cell viability and oxidant stress of Streptococcus thermophilus during cold stage
    Chen, Xu
    Li, Ling
    Yang, Fujia
    Wu, Jinhong
    Wang, Shaoyun
    [J]. FOOD AND CHEMICAL TOXICOLOGY, 2020, 136
1234