Structural and biochemical properties of silver carp surimi as affected by comminution method

Tao Yin; Yating He; Lulu Liu; Liu Shi; Shanbai Xiong; Juan You; Yang Hu; Qilin Huang

doi:10.1016/j.foodchem.2019.02.066

Structural and biochemical properties of silver carp surimi as affected by comminution method

Food Chem. 2019 Jul 30:287:85-92. doi: 10.1016/j.foodchem.2019.02.066. Epub 2019 Feb 21.

Authors

Tao Yin¹, Yating He², Lulu Liu³, Liu Shi⁴, Shanbai Xiong⁵, Juan You⁵, Yang Hu⁵, Qilin Huang⁵

Affiliations

¹ College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China; National R & D Branch Center for Conventional Freshwater Fish Processing, Wuhan, Hubei Province 430070, PR China. Electronic address: yintao@mail.hzau.edu.cn.
² College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China.
³ National R & D Branch Center for Conventional Freshwater Fish Processing, Wuhan, Hubei Province 430070, PR China.
⁴ Institute of Agricultural Products Processing and Nuclear-agricultural Technology, Hubei Academy of Agricultural Sciences, Wuhan, Hubei Province 430064, PR China.
⁵ College of Food Science and Technology, Huazhong Agricultural University, Wuhan, Hubei Province 430070, PR China; National R & D Branch Center for Conventional Freshwater Fish Processing, Wuhan, Hubei Province 430070, PR China.

PMID: 30857722
DOI: 10.1016/j.foodchem.2019.02.066

Abstract

Effects of two typical comminution methods (shearing and blending) on structural and biochemical properties of silver carp surimi were comparatively investigated. Surimi myofibrils in striated appearance were progressively disrupted within 15 min of blending. The myofibrils were completely disintegrated after shearing for 5 min. Surface hydrophobicity of surimi increased and then gradually decreased (p < 0.05) under shearing, while it continuously increased (p < 0.05) under blending. As shearing time was extended, α-helical structure decreased and β-sheet structure increased simultaneously; surface active sulfhydryl content (SH) increased and then decreased (p < 0.05); and intensity of myosin heavy chain (MHC) was gradually reduced. However, secondary structure, MHC intensity and SH were slightly changed as blending time extended. Ca²⁺-ATPase activities increased and then declined (p < 0.05) with transition times at 1 min and 5 min under shearing and blending, respectively. Results indicated that shearing disrupted the ultrastructure and changed biochemical properties of surimi more pronouncedly than blending.

Keywords: 1-Anilino-8-napthalenesulfonate (PubChem CID: 1369); 5, 5-Dithiobis (2-nitrobenzoic acid) (PubChem CID: 6254); Acetone (PubChem CID: 180); Adenosine triphosphate (PubChem CID: 5957); Ca(2+)-ATPase; Comminution; Conformational structure; Glutaraldehyde (PubChem CID: 3485); Myofibrillar protein; Surface hydrophobicity.

MeSH terms

Animals
Carps*
Fish Products / analysis*
Hydrophobic and Hydrophilic Interactions
Myofibrils / chemistry
Myosin Heavy Chains / chemistry
Protein Structure, Secondary

Substances

Myosin Heavy Chains