Environmental Concentrations of Herbicide Prometryn Render Stress-Tolerant Corals Susceptible to Ocean Warming.

Global warming has caused the degradation of coral reefs around the world. While stress-tolerant corals have demonstrated the ability to acclimatize to ocean warming, it remains unclear whether they can sustain their thermal resilience when superimposed with other coastal environmental stressors. We report the combined impacts of a photosystem II (PSII) herbicide, prometryn, and ocean warming on the stress-tolerant coral Galaxea fascicularis through physiological and omics analyses. The results demonstrate that the heat-stress-induced inhibition of photosynthetic efficiency in G. fascicularis is exacerbated in the presence of prometryn. Transcriptomics and metabolomics analyses indicate that the prometryn exposure may overwhelm the photosystem repair mechanism in stress-tolerant corals, thereby compromising their capacity for thermal acclimation. Moreover, prometryn might amplify the adverse effects of heat stress on key energy and nutrient metabolism pathways and induce a stronger response to oxidative stress in stress-tolerant corals. The findings indicate that the presence of prometryn at environmentally relevant concentrations would render corals more susceptible to heat stress and exacerbate the breakdown of coral Symbiodiniaceae symbiosis. The present study provides valuable insights into the necessity of prioritizing PSII herbicide pollution reduction in coral reef protection efforts while mitigating the effects of climate change.

Comparison of three palm tree peroxidases expressed by Escherichia coli: Uniqueness of African oil palm peroxidase.

Palm tree peroxidase has greater catalytic activity, stability and broad application prospects in comparison with horseradish peroxidase. However, slow growth, ecological destruction and high costs prohibit isolation of native peroxidases directly from palm trees. Bioreactor production of palm tree peroxidases would therefore be preferred to overcome such production limitations. Comparison of different recombinant glycan-free palm tree peroxidases would allow understanding the criticality of total glycans to the functions and characteristics. In the present study, African oil palm tree peroxidase expressed by Escherichia coli showed similar stability and 30-100-fold greater activity than that of recombinant royal palm tree peroxidases, but both of their comprehensive indexes were superior to the commercial, native horseradish peroxidase. Recombinant Chamaerops excelsa peroxidase showed no activity possibly due to incorrect protein folding. The results confirmed that recombinant expression by E. coli is potentially an effective means to obtain a mass of palm peroxidases with high activity and stability.