ArticleFood chemistry: X2024
Effects of different protein cross-linking degrees on physicochemical and subsequent thermal gelling properties of silver carp myofibrillar proteins sol subjected to freeze-thaw cycles.
Article in Food chemistry: X, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed.
- Mechanism of Malondialdehyde-Induced Deterioration in Water-Holding Capacity of Bovine Myofibrillar Proteins: Insights from Structural Modifications and Molecular Docking.Foods (Basel, Switzerland) · 2026Article
- Ultrasound-Assisted Curdlan Curing Reduces Water Loss of Rabbit Meat: Water Retention Performance, Myofibrillar Protein Structure, and Processing Adaptability.Foods (Basel, Switzerland) · 2026Article
- Effect of the Number of Gallate Groups of Polyphenols on the Structure, Gel Properties, and Biological Activity of Soy Protein Fibrils.Foods (Basel, Switzerland) · 2025Article
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Authors and funding
5 authors.
Funding
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Abstract
Knowledge regarding the denaturation process and control methods for depolymerized sol-state myofibrillar proteins (MPs) during freezing remains scant. This study investigated the effects of protein cross-linking treatment before freezing on physicochemical and subsequent gelation properties of MPs sol subjected to freeze-thaw (F-T) cycles. Results indicated that after five F-T cycles, cross-linked MPs sols showed increased high molecular weight polymers and bound water (T
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