The synergistic potential of plant essential oils (EOs) with other conventional and non-conventional antimicrobial agents is a promising strategy for increasing antimicrobial efficacy and controlling foodborne pathogens. Spoilage microorganisms are one of main concerns of seafood products, while the prevention of seafood spoilage principally requires exclusion or inactivation of microbial activity. This review provides a comprehensive overview of recent studies on the synergistic antimicrobial effect of EOs combined with other available chemicals (such as antibiotics, organic acids, and plant extracts) or physical methods (such as high hydrostatic pressure, irradiation, and vacuum-packaging) utilized to reduce the growth of foodborne pathogens and/or to extend the shelf-life of seafood products. This review highlights the synergistic ability of EOs when used as a seafood preservative, discovering the possible routes of the combined techniques for the development of a novel seafood preservation strategy.

Microcystin-LR (MC-LR) is prevalent in water and can be translocated into soil-crop ecosystem via irrigation, overflow (pollution accident), and cyanobacterial manure applications, threatening agricultural production and human health. However, the effects of various input pathways on the bioaccumulation and toxicity of MCs in terrestrial plants have been hardly reported so far. In the present study, pot experiments were performed to compare the bioaccumulation, toxicity, and health risk of MC-LR as well as its degradation in soils among various treatments with the same total amount of added MC-LR (150 μg/kg). The treatments included irrigation with polluted water (IPW), cultivation with polluted soil (CPS), and application of cyanobacterial manure (ACM). Three common leaf-vegetables in southern China were used in the pot experiments, including Ipomoea batatas L., Brassica juncea L., and Brassica alboglabra L. All leaf vegetables could bioaccumulate MC-LR under the three treatments, with much higher MC-LR bioaccumulation, especially root bioconcentration observed in ACM treatment than IPW and CPS treatments. An opposite trend in MC-LR degradation in soils of these treatments indicated that ACM could limit MC-LR degradation in soils and thus promote its bioaccumulation in the vegetables. MC-LR bioaccumulation could cause toxicity to the vegetables, with the highest toxic effects observed in ACM treatment. Similarly, bioaccumulation of MC-LR in the edible parts of the leaf-vegetables posed 1.1~4.8 fold higher human health risks in ACM treatment than in IPW and CPS treatments. The findings of this study highlighted a great concern on applications of cyanobacterial manure.

Microbial degradation has been confirmed as effective and environmentally friendly approach to remediate phthalates from the environment, and hydrolase is an effective element for contaminant degradation. In the present study, a novel dibutyl phthalate (DBP)-hydrolyzing carboxylesterase (named PS06828) from Pseudomonas sp. PS1 was heterogeneously expressed in E. coli, which was identified as a new member of the lipolytic family VI. Purified PS06828 could efficiently degrade DBP with a wide range of temperature (25-37 °C) and pH (6.5-9.0). Multi-spectroscopy methods combined with molecular docking were employed to study the interaction of PS06828 with DBP. Fluorescence and UV-visible absorption spectra revealed the simultaneous presence of static and dynamic component in the fluorescence quenching of PS06828 by DBP. Synchronous fluorescence and circular dichroism spectra showed inconspicuous alteration in micro-environmental polarity around amino acid residues but obvious increasing of α-helix and reducing of β-sheet and random coil in protein conformation. Based on the information on exact binding sites of DBP on PS06828 provided by molecular docking, the catalytic mechanism mediated by key residues (Ser113, Asp166, and His197) was proposed and subsequently confirmed by site-directed mutagenesis. The results can strengthen our mechanistic understanding of family VI esterase involved in hydrolysis of phthalic acid esters, and provide a solid foundation for further enzymatic modification.