Globally, the strawberry is one of the most widely consumed fruits, but under certain environmental conditions, it exhibits inadequate red color development, causing economic losses due to lower product quality. In order to evaluate if changes in color are cultivar-specific and environmentally dependent, a comparative study of anthocyanin accumulation, total phenolic, total flavonoid content analysis and additionally a transcriptional profile of pigment-related genes in “Camarosa,” “Cristal,” “Monterey,” and “Portola” (four strawberry cultivars) was performed. These showed an increase in their red coloration during fruit development. The anthocyanin accumulation in the four cultivars was related to the particular progress of the transcriptional activity of genes involved in the biosynthesis of flavonoid pigments. The greatest increase was observed in “Monterey” and “Camarosa”; thus, we have found a correlation between fruit color redness and total anthocyanins only in these cultivars. However, a positive correlation between the mRNA abundance of FaF3′H and FaFLS and the total flavonoids content was found in all cultivars at early stages of ripening. Finally, we found correlations between color and other important physiological properties such as SSC/TA, weight, and aroma expressed as total esters. These results could be useful in making decisions in future breeding programs to improve the content of healthy compound content in strawberry fruit.

Alcohol acyltransferases (AAT) play a key role in ester biosynthesis. In Cucumis melo var. cantalupensis, AATs are encoded by a gene family of four members (CmAAT1–4). CmAAT1, CmAAT3 and CmAAT4 are capable of synthesizing esters, with CmAAT1 the most active. CmAAT2 is inactive and has an Ala268 residue instead of a threonine which is present in all other active AATs, although the role of this residue is still unclear. The present work aims to understand the molecular mechanism involved in ester biosynthesis in melon fruit and to clarify the importance of the Ala268 residue. First, structural models for each protein were built by comparative modelling methodology. Afterwards, conformational interaction between the protein and several ligands, alcohols and acyl‐CoAs was explored by molecular docking and molecular dynamics simulation. Structural analysis showed that CmAATs share a similar structure. Also, well‐defined solvent channels were described in the CmAATs except for CmAAT2 which does not have a proper channel and instead has a small pocket around Ala268. Residues of the catalytic HxxxD motif interact with substrates within the solvent channel, with Ser363 also important. Strong binding interaction energies were described for the best substrate couple of each CmAAT (hexyl‐, benzyl‐ and cinnamyl‐acetate for CmAAT1, 3 and 4 respectively). CmAAT1 and CmAAT2 protein surfaces share similar electrostatic potentials; nevertheless the entrance channels for the substrates differ in location and electrostatic character, suggesting that Ala268 might be responsible for that. This could partly explain the major differences in activity reported for these two enzymes.Database: Structural data have been deposited in the Protein Model Data Bank under the following accession numbers: CmAAT1 (PM0078514); CmAAT2 (PM0078515); CmAAT3 (PM0078516); CmAAT4 (PM0078517)