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Changes in Transglutaminase Activity and Its Contribution to Gelation Properties of Low-Salt Myosin Under Ultrasound.
- Source :
-
Food & Bioprocess Technology . Aug2024, Vol. 17 Issue 8, p2253-2264. 12p. - Publication Year :
- 2024
-
Abstract
- This study explored the changes in cross-linking of low-salt myosin mediated by microbial transglutaminase (MTGase) under high intensity ultrasound (HIU). HIU activated the fish endogenous transglutaminase by 14.11%. Meanwhile, HIU induced the conformational changes in low-salt myosin with decrease of α-helix and increase of β-sheet structures. At 0.1 mol/L salt, compared to solely treated MTGase/solely treated myosin, the most ε-(γ-Glu)-Lys bonds were formed in HIU-treated MTGase + myosin, evidenced by the lowest solubility. Correspondingly, the G' showed the highest increase rate. Consequently, the samples formed regular and continuous protein matrix structures. Specifically, the microstructures of HIU-treated MTGase + myosin samples at 0.1 mol/L salt were even more compact than those of control samples at 0.3 mol/L salt. Besides, HIU-treated MTGase + myosin improved the water holding capacity by 18.28%. In summary, HIU promoted the cross-linking between low-salt myosin mediated by MTGase through activating the enzyme, improving substrate dispersion, or both, with the largest improvement degree observed for HIU-treated MTGase + myosin group. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 19355130
- Volume :
- 17
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Food & Bioprocess Technology
- Publication Type :
- Academic Journal
- Accession number :
- 178528122
- Full Text :
- https://doi.org/10.1007/s11947-023-03250-7