Modification of myofibrillar protein structural characteristics: Effect of ultrasound-assisted first-stage thermal treatment on unwashed Silver Carp surimi gel

Yisha Xie; Kangyu Zhao; Feng Yang; Wenjing Shu; Junkun Ma; Yizhen Huang; Xi Cao; Qingqing Liu; Yongjun Yuan

doi:10.1016/j.ultsonch.2024.106911

Modification of myofibrillar protein structural characteristics: Effect of ultrasound-assisted first-stage thermal treatment on unwashed Silver Carp surimi gel

Ultrason Sonochem. 2024 May 15:107:106911. doi: 10.1016/j.ultsonch.2024.106911. Online ahead of print.

Authors

Yisha Xie¹, Kangyu Zhao², Feng Yang², Wenjing Shu², Junkun Ma², Yizhen Huang³, Xi Cao², Qingqing Liu², Yongjun Yuan⁴

Affiliations

¹ Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China. Electronic address: Isabella-xie@foxmail.com.
² Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China.
³ College of Food Science and Nutritional Engineering, China Agricultural University, Beijing 100083, China.
⁴ Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, School of Food and Bioengineering, Xihua University, Chengdu 610039, Sichuan, China. Electronic address: yyja9791@sina.com.

Abstract

The hardness properties of unwashed surimi gel are considered as the qualities of gelation defect. This research investigated the effect of ultrasound-assisted first-stage thermal treatment (UATT) on the physicochemical properties of unwashed Silver Carp surimi gel, and the enhancement mechanism. UATT could reduce protein particle size, which significantly reduced from 142.22 μm to 106.70 μm after 30 min of UATT compared with the nature protein. This phenomenon can promote the protein crosslinking, resulting in the hardness of surimi gel increased by 15.08 %. Partially unfolded structure of myofibrillar protein and exposures of tryptophan to water, lead to the increase in the zeta potential absolute value, driven by UATT. The reduced SH group level and the conformational conversion of proteins from random coiling to α-helix and β-sheet, which was in support of intermolecular interaction and gel network construction. The results are valuable for processing protein gels and other food products.

Keywords: Myofibrillar protein; Two-stage heating; Ultrasound; Unwashed surimi gel.