Myoglobin Post-Translational Modifications Influence Color Stability of Beef Longissimus Lumborum

نویسندگان

چکیده

Post-translational modifications (PTM) of proteins play critical roles in biological processes. PTM muscle influence meat quality. Nonetheless, myoglobin (Mb) and their impact on fresh beef color stability have not been characterized yet. Therefore, our objectives were to identify Mb longissimus lumborum during postmortem aging characterize stability. The muscles from 9 (n = 9) carcasses (24 h postmortem) subjected wet for 0, 7, 14, 21 d. At the end each wet-aging period, steaks fabricated. One steak analyses was immediately frozen at ?80°C, whereas other assigned refrigerated storage darkness under aerobic packaging. Instrumental biochemical attributes evaluated day 3, or 6 storage. analyzed using two-dimensional electrophoresis tandem mass spectrometry. Surface redness (a* value), stability, concentration decreased (P < 0.05) upon aging. Gel image identified spots with similar molecular weight (17 kDa) but different isoelectric pH. Tandem spectrometry multiple (phosphorylation, methylation, carboxymethylation, acetylation, 4-hydroxynonenal alkylation) these isoforms. amino acids susceptible phosphorylation serine (S), threonine (T), tyrosine, detected lysine (K), arginine (R), histidine residues. Additionally, distal (position 64), heme found be alkylated. Overall, increased aging-induced PTM, especially those occurring close hydrophobic pocket, could disrupt tertiary structure, affinity, compromise oxygen binding capacity, leading beef. Furthermore, K45, K47, K87 unique non-aged beef, R31, T51, K96, K98, S121, R139, K147 aged counterparts, indicating that used as novel biomarkers

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ژورنال

عنوان ژورنال: Meat and muscle biology

سال: 2021

ISSN: ['2575-985X']

DOI: https://doi.org/10.22175/mmb.11689