ArticleFood chemistry: X2025
Proteolytic and structural mechanisms in tuna tenderization by papain, bromelain and ficin.
Article in Food chemistry: X, 2025. 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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Who cites it
3 citing papers in PubMed.
- Exploration of the mechanism of key odour substances in porcine large intestine by enzyme-alkali-alcohol ternary composite treatment: Efficacy of deodorisation treatments and impact on quality.Food chemistry: X · 2026Article
- Proteolytic Tenderization of Pork Loin with Papain and Bromelain and Its Physicochemical and Sensory Effects.Foods (Basel, Switzerland) · 2026Article
- Biopolymer Development from Agro-Food and Aquaculture By-Products with Antioxidant Hydrolysates ofInternational journal of molecular sciences · 2025Article
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Authors and funding
9 authors.
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Abstract
Thermal processing could reduce tenderness of cooked tuna. Papain, bromelain and ficin were employed to solve this issue, and their tenderizing mechanisms were investigated. Protein profiles showed that macromolecular proteins in tuna were degraded into smaller fractions by proteases, which led to increases in the myofibrillar fragmentation index (MFI) values. All proteases reduced shear force and hardness but increased cooking loss of tuna (except ficin), accompanied by the formation of unevenly distributed pores in tuna microstructures. Compared with control, bromelain decreased shear force and hardness by 86.95 % and 58.25 %, showing the best tenderizing effect. Moreover, reduction in content of disulfide bonds, the primary molecular force in tuna network, also contributed to the improvement of tenderness. Additionally, the ordered structures (α-helix and β-sheet) were transformed to disordered structures (β-turn and random coil) by proteases. These findings showed that proteases could significantly enhance the tenderness of tuna, especially bromelain.
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