The effects of (E)‐2‐hexenal on morphological, physiological, and biochemical indices of postharvest disease Penicillium cyclopium spores

Abstract

The study investigated the effects of (E)‐2‐hexenal on morphology and function of Penicillium cyclopium spores, and these conidia were treated with (E)‐2‐hexenal at various concentrations. (E)‐2‐hexenal at 8× minimum fungicidal concentration (8× MFC, 2560 μl/L) severely damaged conidia membranes through scanning electron microscopy, which resulted in the changes in membrane permeability parameters including the release of intracellular adenosine triphosphate content, loss of 260 nm‐absorbing materials, and the decrease of extracellular pH, the increase in extracellular conductivity, and membrane leakage as determined by propidium iodide staining. (E)‐2‐hexenal (≤2 × MFC, 640 μl/L) always induced superoxide dismutase and catalase enzyme activities in P. cyclopium conidia. These results suggest that (E)‐2‐hexenal damages fungal spore membranes, and inhibit spore germination in a dose‐dependent manner, causing a series of changes in membrane permeability parameters, which serves as the inhibitory mechanism of (E)‐2‐hexenal against P. cyclopium. Practical applications (E)‐2‐hexenal treatment significantly resulted in serious detrimental damages in the morphology and function in P. cyclopium spores. The work presented (E)‐2‐hexenal could control fungal pathogens through disruption of cell membrane integrity and membrane permeability. The results revealed that (E)‐2‐hexenal can be used as a new anti‐fungal agent against P. cyclopium.

Antifungal mechanism of (E)-2-hexenal against Botrytis cinerea growth revealed by transcriptome analysis

“…Terpenoid has the lipophilic property, so it can preferentially enter into the lipid membrane, which leads to increasing fluidity of the bilayer lipid membrane and ultimately increasing membrane permeability ( Xu et al, 2017 ). ( E )-2-hexenal could constrain fungal pathogens by disrupting the integrity and permeability of the cell membrane ( Ma et al, 2019 ).…”

Green Leaf Volatile Trans-2-Hexenal Inhibits the Growth of Fusarium graminearum by Inducing Membrane Damage, ROS Accumulation, and Cell Dysfunction

“…F. graminearum mycelia were induced and treated with T2H in accordance with the procedure described in mycelial biomass assay, and then the electrolyte leakage was measured by a conductivity meter (INESA Scientific Instrument Co., Ltd., China) to evaluate the disturbance of membrane permeability by T2H, and the MDA content was determined by the thiobarbituric acid (TBA) method to quantify lipid peroxidation. , The concentration of T2H was adjusted to 0 μL/mL as the control. All experiments consisted of three technical replicates and were independently repeated three times.…”

“…T2H triggered great damage to the Penicillium cyclopium spore membrane, resulting in the leakage of intracellular adenosine triphosphate (ATP), nucleic acids, and ions and increased catalase (CAT) and superoxide dismutase (SOD) activities. 20 Similarly, the application of T2H reduced intracellular acetyl-coenzyme A (CoA) and soluble protein contents of Aspergillus flavus, interfered with pyruvate metabolism during spore germination, and inhibited mitochondrial dehydrogenase activity. 21 As an electrophile, the α,β-unsaturated carbonyl of T2H may react with the thiol groups of proteins to induce reactive oxygen species (ROS) production.…”

“…Previous studies have characterized the detailed effects of T2H on microbial cell structure and function by means of pharmacological toxicology and microscopic observation. T2H triggered great damage to the Penicillium cyclopium spore membrane, resulting in the leakage of intracellular adenosine triphosphate (ATP), nucleic acids, and ions and increased catalase (CAT) and superoxide dismutase (SOD) activities . Similarly, the application of T2H reduced intracellular acetyl-coenzyme A (CoA) and soluble protein contents of Aspergillus flavus, interfered with pyruvate metabolism during spore germination, and inhibited mitochondrial dehydrogenase activity .…”