Investigating the migration hypothesis: Effects of trypsin-like protease on the quality of muscle proteins of red shrimp (Solenocera crassicornis) during cold storage

Feili Zhan; Zhipeng Li; Daodong Pan; Soottawat Benjakul; Xuepeng Li; Bin Zhang

doi:10.1016/j.fochx.2023.100906

Investigating the migration hypothesis: Effects of trypsin-like protease on the quality of muscle proteins of red shrimp (Solenocera crassicornis) during cold storage

Food Chem X. 2023 Sep 30:20:100906. doi: 10.1016/j.fochx.2023.100906. eCollection 2023 Dec 30.

Authors

Feili Zhan^{1

2}, Zhipeng Li¹, Daodong Pan², Soottawat Benjakul³, Xuepeng Li⁴, Bin Zhang¹

Affiliations

¹ Key Laboratory of Health Risk Factors for Seafood of Zhejiang Province, College of Food Science and Pharmacy, Zhejiang Ocean University, Zhoushan 316022, China.
² College of Food Science and Pharmacy, Ningbo University, Ningbo 315832, China.
³ International Center of Excellence in Seafood Science and Innovation, Faculty of Agro-Industry, Prince of Songkla University, Songkhla 90112, Thailand.
⁴ College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning 121013, China.

Abstract

This study aimed to investigate the effect of trypsin-like protease (TLP) on the quality of muscle proteins in red shrimp (Solenocera crassicornis) during cold storage. The results indicated that the activity of TLP decreased significantly in the head of shrimp but increased significantly in the muscle tissues during the cold storage. The myofibril fragmentation index (MFI) value of intact shrimp was significantly higher than that of beheaded shrimp, while the Ca²⁺-ATPase activity of intact shrimp was significantly lower than that of beheaded shrimp. SDS-PAGE analysis showed that the molecular weight of purified TLP from the shrimp head was about 24 kDa, and the TLP showed high activity at 50 °C and pH 8, indicating that the TLP belongs to the trypsin family. Results from in vitro simulation experiments indicated that the process of TLP incubation significantly reduced the particle size and enlarged the distribution of myofibrillar proteins (MPs) in shrimp muscle tissues. The comparisons were made with respect to the control samples. It can be inferred that TLP migrated from the shrimp head to the muscle tissues during storage and thus promoted the degradation of MPs in red shrimp. The beheading treatment could be an effective mean to maintain better quality and extend the commercialization of shrimp products.

Keywords: Ammonium persulfate (PubChem CID: 62648); Ammonium sulfate (PubChem CID: 6097028); Bromophenol blue (PubChem CID: 8272); Disodium hydrogen phosphate (PubChem CID: 24203); Formaldehyde (PubChem CID: 712); Methyl red (PubChem CID: 10303); Migration; Muscle proteins; Myofibrillar proteins; Red shrimp; Sodium chloride (PubChem CID: 5234); Trichloroacetic acid (PubChem CID: 6421); Trypsin-like protease.