Since the deep cause for the anti-oxidation of carnosic acid (CA) against oleic acid (OA) remains unclear, we focused on exploring the CA inhibition mechanism via a combined experimental and computational study. Atomic charge, total molecular energy, phenolic hydroxyl bond dissociation enthalpy (BDE), the highest occupied molecular orbital (HOMO), and the lowest unoccupied orbital (LUMO) energy were first discussed by the B3LYP/6-31G (d,p) level, a density functional method. A one-step hydrogen atom transfer (HAT) was proposed for the anti-oxidation of CA towards OA, and the Rancimat method was carried out for analyzing the thermal oxidation stability. The results indicate that the two phenolic hydroxyl groups located at C7(O15) and C8(O18) of CA exert the highest activity, and the chemical reaction heat is minimal when HAT occurs. Consequently, the activity of C7(O15) (303.27 kJ/mol) is slightly lower than that of C8(O18) (295.63 kJ/mol), while the dissociation enthalpy of phenol hydroxyl groups is much lower than those of α-CH2 bond of OA (C8, 353.92 kJ/mol; C11, 353.72 kJ/mol). Rancimat method and non-isothermal differential scanning calorimetry (DSC) demonstrate that CA outcompetes tertiary butylhydroquinone (TBHQ), a synthetic food grade antioxidant, both in prolonging the oxidation induction period and reducing the reaction rate of OA. The Ea (apparent activation energies of reaction) of OA, TBHQ + OA, and CA + OA were 50.59, 57.32 and 66.29 kJ/mol, revealing that CA could improve the Ea and thermal oxidation stability of OA.
Ethephon (ETH), a commonly employed growth regulator, poses potential health risks due to its residue in fruits and vegetables, leading to both acute and subchronic toxicity. However, the detection accuracy of ETH is compromised by the color effects of the samples during the detection process. In this work, a multienzyme reaction-mediated electrochemical biosensor (MRMEC) was developed for the sensitive, rapid, and color-interference-resistant determination of ETH. Nanozymes Fe3O4@Au–Pt and graphene nanocomplexes (GN–Au NPs) were prepared as catalysts and signal amplifiers for MRMEC. Acetylcholinesterase (AChE), acetylcholine (ACh), and choline oxidase (CHOx) form a cascade enzyme reaction to produce H2O2 in an electrolytic cell. Fe3O4@Au–Pt has excellent peroxidase-like activity and can catalyze the oxidation of 3,3′,5,5′-tetramethvlbenzidine (TMB) in the presence of H2O2, resulting in a decrease in the characteristic peak current of TMB. Based on the inhibitory effect of ETH on AChE, the differential pulse voltammetry (DPV) current signal of TMB was used to detect ETH, offering the limit of detection (LOD) of 2.01 nmol L−1. The MRMEC method effectively analyzed ETH levels in mangoes, showing satisfactory precision (coefficient of variations, 2.88–15.97%) and recovery rate (92.18–110.72%). This biosensor holds promise for detecting various organophosphorus pesticides in food samples.
Mung bean (Vigna radiate) sprouts are a popular choice among sprouted vegetables in Asia. Currently, the impact of nitrogen sources on the growth of mung bean sprouts remains poorly understood, and the underlying biological mechanisms responsible for the observed nonlinear growth patterns at different nitrogen levels have yet to be elucidated. In this research, in addition to conventional growth monitoring and quality evaluation, a comparative proteomics method was applied to investigate the molecular mechanisms of mung bean in response to 0, 0.025, 0.05, 0.075, and 0.1% urea concentrations. Our results indicated that mung bean sprout height and yield increased with rising urea concentrations but were suppressed beyond the L3 level (0.075% urea). Nitrate nitrogen and free amino acid content rose steadily with urea levels, whereas protein content, nitrate reductase activity, and nitrite levels followed a peak-then-decline trend, peaking at intermediate concentrations. Differential expression protein analysis was conducted on mung bean sprouts treated with different concentrations of urea, and more differentially expressed proteins participated in the L3 urea concentration. Analysis of common differential proteins among comparison groups showed that the mung bean sprouts enhanced their adaptability to urea stress environments by upregulating chlorophyll a-b binding protein and cationic amino acid transporter and downregulating the levels of glycosyltransferase, L-ascorbic acid, and cytochrome P450. The proteomic analysis uncovered the regulatory mechanisms governing these metabolic pathways, identifying 47 differentially expressed proteins (DEPs) involved in the biosynthesis of proteins, free amino acids, and nitrogen-related metabolites.