Abstract
Theoretical and experimental studies were conducted to determine the role of 1-MCP in the biosynthesis of ethylene in cape gooseberry fruits (Physalis peruviana L.), ecotype Colombia. A completely randomized experimental design was used with 3 treatments: ethylene (1000 μL ethephon L−1), 1-MCP (1 μL L−1), and a control with no applications. At 1, 6 and 11 days after treatment, volatile compounds, firmness and color were measured. The enzymatic activities of ACC oxidase (E.C. 1.14.17.4) and histidine kinase (HK, E.C. 2.7.13.3) were also determined in vitro. Subsequently, molecular docking studies with the enzymes, their respective substrates and 1-MCP were carried out. It was found that 1-MCP decreased the emission of volatile esters, color index, loss of firmness, and ACC oxidase and histidine kinase activities. Results indicated 1-MCP acted as a competitive inhibitor of ACC oxidase and as a noncompetitive inhibitor of HK. The coupling free energy was higher for 1-MCP in both the ACC oxidase (8.31) and the HK (4.22), compared to their respective substrates. The results also suggested that 1-MCP was able to decrease both the biosynthesis and activity of ethylene in cape gooseberry fruits.
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