Insights into the similarities and differences of whiteleg shrimp pre-soaked with sodium tripolyphosphate and sodium trimetaphosphate during frozen storage

• Published in: Food chemistry Vol. 348; p. 129134
• Main Authors: Ying, Xiao-guo, Wu, Qiong-jing, Shui, Shan-shan, Zhang, Bin, Benjakul, Soottawat
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 30-06-2021
• Subjects: Animals; Chromatography, High Pressure Liquid; Food Storage - methods; Freezing; Frozen storage; Heat-Shock Proteins - metabolism; Label-free proteomics; Penaeidae - chemistry; Penaeidae - metabolism; Peptides - analysis; Polyphosphates - chemistry; Protein stability; Seafood - analysis; Shellfish Proteins - metabolism; Shrimp; Sodium trimetaphosphate (STMP); Sodium tripolyphosphate (STPP); Tandem Mass Spectrometry; Time Factors; Protein stability; Frozen storage; Sodium trimetaphosphate (STMP); Shrimp; Sodium tripolyphosphate (STPP); Label-free proteomics
• ISSN: 0308-8146; 1873-7072
• DOI: 10.1016/j.foodchem.2021.129134

•Similarities and differences in shrimp pre-soaked with STPP and STMP were investigated during storage.•STMP and STPP maintained the WHC, texture, and thermal stability of muscle proteins.•STMP exhibited better protective abilities than STPP after 12 weeks of storage.•STMP upregulated several cytoskeleton and ribosomal proteins compared to STPP.
In this study, similarities and differences of sodium tripolyphosphate (STPP) and sodium trimetaphosphate (STMP) pre-soaking on the stability of muscle proteins in shrimp were investigated during 12 weeks of frozen storage (−30 °C). The physicochemical analysis indicated significant improvements in the WHC, springiness, chewiness, and thermal stability of STPP and STMP pre-soaked samples when compared to the control. Interestingly, STMP pre-soaking showed better cryoprotective effects than the STPP treatment when the storage period reached the end of the 12 weeks. Furthermore, the label-free based proteomics results indicated that 62 upregulated differentially abundant proteins (DAPs) were detected in STMP when compared to STPP. These identified DAPs specifically included 40S ribosomal proteins, actin-related proteins, heat shock proteins, myosin heavy chain, and tubulin beta chain. Additionally, the gene ontology (GO) and eukaryotic clusters of orthologous group (KOG) analyses verified that the incorporation of STMP molecules enhanced the resistance of cytoskeleton proteins to cold-temperature stress.