Identification and characterization of phosphoproteins in the striated and smooth adductor muscles of Yesso scallop Patinopecten yessoensis.
Glycolytic enzymes
Meat quality
Myofibrillar proteins
Protein phosphorylation
Scallop
Journal
Food chemistry
ISSN: 1873-7072
Titre abrégé: Food Chem
Pays: England
ID NLM: 7702639
Informations de publication
Date de publication:
15 Mar 2022
15 Mar 2022
Historique:
received:
24
05
2021
revised:
08
09
2021
accepted:
24
09
2021
entrez:
25
11
2021
pubmed:
26
11
2021
medline:
27
11
2021
Statut:
ppublish
Résumé
Many proteins are known to be phosphorylated, affecting important regulatory factors of muscle quality in the aquatic animals. The striated and smooth adductor muscles of Yesso scallop Patinopecten yessoensis were used to investigate muscle texture and identify phosphoproteins by histological methods and phosphoproteomic analysis. Our present study reveals that muscle fiber density is in relation to meat texture of the striated and smooth adductor muscles. The phosphoproteomic analysis has identified 764 down-regulated and 569 up-regulated phosphosites on 743 phosphoproteins in the smooth muscle compared to the striated part. The identification of unique phosphorylation sites in glycolytic enzymes may increase the activity of glycolytic enzymes and the rate of glycolysis in the striated adductor muscle. The present findings will provide new evidences on the role of muscle structure and protein phosphorylation in scallop muscle quality and thus help to develop strategies for improving meat quality of scallop products.
Identifiants
pubmed: 34818726
pii: S0308-8146(21)02248-2
doi: 10.1016/j.foodchem.2021.131242
pii:
doi:
Substances chimiques
Phosphoproteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
131242Informations de copyright
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