The UHPLC-HRMS method described was successful in rapidly profiling phlorotannins in brown seaweeds based on their degree of polymerisation. HILIC was demonstrated to be an effective separation mode, particularly for low molecular weight phlorotannins.

BACKGROUND: Several studies have demonstrated the feasibility of treating aqueous phenols and aromatic amines with oxidoreductases in synthetic wastewater samples. However, little work has been done on the effectiveness of enzymatic treatment on real wastewater. Here a comparison was made of the oxidative coupling of phenol catalyzed by laccase or soybean peroxidase (SBP) using synthetic and refinery wastewaters.

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The potential of oxidoreductases, such as laccases and peroxidases, to remove organic pollutants from industrial wastewater and process water is addressed in this short review, with an emphasis on the peroxidase work completed or in progress in the authors’ laboratory. The major drawback to this treatment is the cost of the enzyme. However, with new sources and recent advances in the biotechnology industry, it is becoming a feasible alternative. A niche where enzymatic treatment may be first applied is not as a primary treatment but as a secondary treatment (pretreatment or polishing) coupled to existing physico-chemical or biological processes to increase their overall efficiency and economy. Soybean seed coat peroxidase is well suited because of its stability, ease of extraction, widespread availability and potential for adding to the soy value chain. Since crude enzyme often works better than purified enzyme, the only additional cost may be in concentrating the extract. This review briefly covers aspects of the enzymatic treatment such as cost, use of additives for increased enzyme economy, enzyme recycling and studies already completed on industrial wastewaters.

Daphnia pulex is a keystone species for aquatic habitats and an ecological/evolution model organism. Although significant progress has been made on characterizing its genome, the D. pulex proteome remains largely uncharacterized partially due to abnormally high protein degradation during homogenization and emphasis on genomic analysis. In this study, various sample preparation and mass spectrometry acquisition methods are performed for the purpose of improving D. pulex proteome exploration. Benefits for employing both in-gel and in-solution methods of trypsin digestion are observed. Furthermore, acquisition methods employing ion mobility separation greatly increase peptide identification and more than doubled the proteome coverage. Bioinformatic analysis suggests that mitochondrial and hydrolytic activities are enriched in D. pulex compared to closely related invertebrates or Homo sapiens. Also, novel D. pulex proteins possessing putative genome modifying functional domains are identified. Data are available via ProteomeXchange with identifier PXD008455.