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dc.contributor.authorSaez, Darwin
dc.contributor.authorRodríguez-Arriaza, Francisca
dc.contributor.authorUrra, Gabriela
dc.contributor.authorFabi, João Paulo
dc.contributor.authorHormazábal-Abarza, Francisca
dc.contributor.authorMéndez-Yáñez, Angela
dc.contributor.authorCastro, Egle
dc.contributor.authorBustos, Daniel
dc.contributor.authorRamos, Patricio
dc.contributor.authorMorales-Quintana, Luis
dc.date.accessioned2024-06-19T04:43:04Z
dc.date.available2024-06-19T04:43:04Z
dc.date.issued2024
dc.identifier10.1016/j.plaphy.2024.108668
dc.identifier.issn09819428
dc.identifier.urihttps://hdl.handle.net/20.500.12728/11332
dc.description.abstractAlcohol acyltransferases (AATs) play a crucial role in catalyzing the transfer of acyl groups, contributing to the diverse aroma of fruits, including strawberries. In this research we identified nine AAT genes in strawberries through a comprehensive analysis involving phylogenetics, gene structure, conserved motifs, and structural protein model examinations. The study used the ‘Camarosa’ strawberry genome database, and experiments were conducted with fruits harvested at different developmental and ripening stages. The transcriptional analysis revealed differential expression patterns among the AAT genes during fruit ripening, with only four genes (SAAT, FaAAT2, FaAAT7, and FaAAT9) showing increased transcript accumulation correlated with total AAT enzyme activity. Additionally, the study employed in silico methods, including sequence alignment, phylogenetic analysis, and structural modeling, to gain insights into the AAT protein model structures with increase expression pattern during fruit ripening. The four modeled AAT proteins exhibited structural similarities, including conserved catalytic sites and solvent channels. Furthermore, the research investigated the interaction of AAT proteins with different substrates, highlighting the enzymes' promiscuity in substrate preferences. The study contributes with valuable information to unveil AAT gene family members in strawberries, providing scientific background for further exploration of their biological characteristics and their role in aroma biosynthesis during fruit ripening. © 2024 Elsevier Masson SASes_ES
dc.description.sponsorshipFondo Nacional de Desarrollo Científico y Tecnológico, FONDECYT, (1220782, 3220284, 1211057, 11220444, FOVI230136, 21241441); Fondo Nacional de Desarrollo Científico y Tecnológico, FONDECYT; Agencia Nacional de Investigación y Desarrollo, ANID, (190093); Agencia Nacional de Investigación y Desarrollo, ANIDes_ES
dc.language.isoenes_ES
dc.publisherElsevier Masson s.r.l.es_ES
dc.subjectAlcohol acyltransferasees_ES
dc.subjectEster biosynthesises_ES
dc.subjectFragaria x ananassaes_ES
dc.subjectFruit ripening processes_ES
dc.subjectMolecular dynamic simulationes_ES
dc.titleUnraveling the key step in the aroma puzzle: Insights into alcohol acyltransferases in strawberrieses_ES
dc.typeArticlees_ES


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