Abiotic and biotic stresses induce the formation of reactive oxygen species (ROS), which subsequently causes the excessive accumulation of aldehydes in cells. Stress-derived aldehydes are commonly designated as reactive electrophile species (RES) as a result of the presence of an electrophilic α, β-unsaturated carbonyl group. Aldehyde dehydrogenases (ALDHs) are NAD(P)⁺-dependent enzymes that metabolize a wide range of endogenous and exogenous aliphatic and aromatic aldehyde molecules by oxidizing them to their corresponding carboxylic acids. The ALDH enzymes are found in nearly all organisms, and plants contain fourteen ALDH protein families. In this review, we performed a critical analysis of the research reports over the last decade on plant ALDHs. Newly discovered roles for these enzymes in metabolism, signaling and development have been highlighted and discussed. We concluded with suggestions for future investigations to exploit the potential of these enzymes in biotechnology and to improve our current knowledge about these enzymes in gene signaling and plant development.

In this article, we have reported an environmentally benign and cost-effective method for the synthesis of monodispersed silver nanoparticles (AgNPs), based on Centella asiatica phenolic extracts (CAPE). The presence of phenolics was confirmed by ultra high-performance liquid chromatography coupled with electrospray ionization quadrupole time of flight mass spectrometry (UHPLC-ESI-qTOF-MS). Colloidal AgNPs synthesized under different concentrations of silver nitrate were monitored with a UV-vis spectrophotometer. Maximum absorption spectra intensity was found to range between 430–440 nm, during a synthesis time of 90 minutes at room temperature. The as-synthesized CAPE-AgNPs, was subjected to various instrumental characterizations such as, transmission electron microscopy (TEM), X-ray powder diffraction (XRD), energy dispersive X-ray spectroscopy (EDS), Fourier transform infrared (FTIR) spectroscopy, dynamic light scattering (DLS) and zeta potential. At the optimized synthesis conditions, spherical and monodispersed CAPE-AgNPs were obtained, with an absorption maximum at 430 nm. The crystalline CAPE-AgNPs had a face-centered-cubic (fcc) crystallographic structure, possessing average sizes estimated from TEM, to be between 20–25 nm diameter, a hydrodynamic diameter from DLS of about 90 nm and a zeta potential value of −28.7 mV. FTIR results validated the presence of phenolics on the surfaces of CAPE-AgNPs. The anti-microbial capacity of CAPE-AgNPs was further demonstrated on different pathogenic bacterial strains with satisfactory performances. As a result of the high surface area to volume ratio of CAPE-AgNPs, it was investigated as a catalyst towards the reduction of prominent environmental pollutants, 4 nitrophenol (4 NP), Congo red (CR) and methylene blue (MB). Pseudo first order kinetics were obtained with rate constants of 3.9 × 10⁻³ s⁻¹ for 4 NP, 54.7 × 10⁻³ min⁻¹ for MB and 5.6 × 10⁻³ s⁻¹ for CR. The catalytic performance and antimicrobial activities of CAPE-AgNPs suggest its potential application in wastewater treatment and control of pathogenic microbes.

Plants are sessile in nature and they perceive and react to environmental stresses such as abiotic and biotic factors. These induce a change in the cellular homeostasis of reactive oxygen species (ROS). ROS are known to react with cellular components, including DNA, lipids, and proteins, and to interfere with hormone signaling via several post-translational modifications (PTMs). Protein carbonylation (PC) is a non-enzymatic and irreversible PTM induced by ROS. The non-enzymatic feature of the carbonylation reaction has slowed the efforts to identify functions regulated by PC in plants. Yet, in prokaryotic and animal cells, studies have shown the relevance of protein carbonylation as a signal transduction mechanism in physiological processes including hydrogen peroxide sensing, cell proliferation and survival, ferroptosis, and antioxidant response. In this review, we provide a detailed update on the most recent findings pertaining to the role of PC and its implications in various physiological processes in plants. By leveraging the progress made in bacteria and animals, we highlight the main challenges in studying the impacts of carbonylation on protein functions in vivo and the knowledge gap in plants. Inspired by the success stories in animal sciences, we then suggest a few approaches that could be undertaken to overcome these challenges in plant research. Overall, this review describes the state of protein carbonylation research in plants and proposes new research avenues on the link between protein carbonylation and plant redox biology.