ArticleFood chemistry: X2023
Improvement in the gelling properties of myofibrillar protein from the razor clam (
Article in Food chemistry: X, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Regulation of Rainbow Trout Muscle Myofibrillar Networks by Non-Enzymatic Bioactive Compounds fromGels (Basel, Switzerland) · 2026Article
- Consequences of ball-milling combined with high-pressure homogenization on structure, physicochemical and functional properties of pea protein.Food chemistry: X · 2025Article
- Modification approaches of walnut proteins to improve their structural and functional properties: A review.Food chemistry: X · 2024Article
- Effect of Boiling Treatment on Linoleic Acid-Induced Oxidation of Myofibrillar Protein in Grass Carp.Foods (Basel, Switzerland) · 2024Article
- Effects ofFoods (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
This study investigated the modification of myofibrillar protein (MP) from the razor clam through phosphorylation by using various phosphate salts, namely, sodium tripolyphosphate (STPP), sodium trimetaphosphate (STMP), sodium polyphosphate (STTP) and sodium pyrophosphate (TSPP), and their mechanisms of action for functional and gelling properties. Fourier transform infrared spectrometry (FTIR) showed that MP introduced phosphate groups during phosphorylation; these phosphates changed the secondary structure. Moreover, MP after phosphorylation led to an increase in solubility, which was more evident in the case of TSPP phosphorylation, leading to the improvement of gel properties. Therefore, TSPP was the phosphate with the best gel properties in the modification of MP, showing the highest phosphorus content, which resulted in better gelling properties owing to its relatively shorter chains. These results showed that phosphate was able to improve protein cross-linking through ion interactions and electrostatic interactions, which ultimately improved the gelling properties of the razor clam protein.
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