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Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
Published on: August 9, 2024
Metmyoglobin cryostability by low molecular weight compounds and their effect on sulfmyoglobin formation by thermal
Juan C Ramírez-Suárez1, Andrés Álvarez-Armenta2, Alonso A López-Zavala3
1Laboratorio de Bioquímica y Calidad de Productos Pesqueros, Tecnología de Alimentos de Origen Animal, Centro de Investigación en Alimentación y Desarrollo, A.C., Hermosillo, Sonora, Mexico.
Abstract:
Meat greening, a pigmentation anomaly linked to thermal treatment, occurs due to sulfmyoglobin (SulfMb) formation, resulting from a reaction between metmyoglobin (MetMb) and free cysteine (Cys). Alternatively, proteins can be denatured after exposure to freezing conditions. A previous study showed that low molecular weight compounds (LMWC) such as arginine (Arg), taurine (Tau), sarcosine (Sar), and trimethylamine oxide (TMAO) presented an apparent protein cryostabilizing activity. Hence, the cryostabilizing effect of these LMWC on MetMb freezing (-18 °C/48 h) was studied by measuring its reactivity with Cys for SulfMb production during thermal treatment (60 °C/30 min, pH 5.7), MetMb solubility, and thermal characterization (by differential scanning calorimetry) of LMWC solutions. Results indicated sarcosine and its combination with taurine protected MetMb during freezing, preserving its solubility (only 1.9 % aggregation) and reactivity (<7 % reduction) to form SulfMb. Results suggest that Sarcosine with/without taurine can be used as a food additive to cryoprotect globular proteins.
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