ABSTRACT
Solar interface evaporation is an effective method for the treatment of water that has low energy consumption. Adsorption is recognized to be one of the most stable wastewater treatment methods and is widely used. Combining solar interface evaporation with adsorption provides a novel and low-cost approach for the efficient removal of heavy metals and organic pollutants from industrial wastewater. This paper reviews the characteristics and application of some common wastewater treatment methods. The photothermal conversion and the conceptual design of interface evaporation combined with adsorption are introduced and the photo-thermal conversion and adsorption methods are discussed. The study provides a summary of recent studies and advancements in interfacial evaporation-coupled adsorption materials, which include hydrogels, aerogels, and biomass materials for adsorption, and carbon materials for photothermal conversion. Finally, the current challenges encountered in industrial wastewater treatment are outlined and its prospects are discussed. The aim of this review is to explore a wide range of possibilities with the interfacial evaporation-coupled adsorption method and propose a new low-cost and high-efficiency method for industrial wastewater treatment.
ABSTRACT
BACKGROUND: A nematophagous fungus, Esteya vermicola, is recorded as the first endoparasitic fungus of pine wood nematode (PWN), Bursaphelenchus xylophilus, in last century. E. vermicola exhibited high infectivity toward PWN in the laboratory conditions and conidia spraying of this fungus on Japanese red pine, Pinus densiflora, seedlings in the field protected the pine trees from pine wilt disease to some extent, indicating that it is a potential bio-control agent against PWN. Previous research had demonstrated that the living fungal mycelia of E. vermicola continuously produced certain volatile organic compounds (VOCs), which were responsible for the PWN attraction. However, identity of these VOCs remains unknown. METHODOLOGY/PRINCIPAL FINDINGS: In this study, we report the identification of α-pinene, ß-pinene, and camphor produced by living mycelia of E. vermicola, the same volatile compounds emitted from PWN host pine tree, as the major VOCs for PWN attraction using gas chromatography-mass spectrometry (GC-MS). In addition, we also confirmed the host deception behavior of E. vermicola to PWN by using synthetic VOCs in a straightforward laboratory bioassay. CONCLUSIONS/SIGNIFICANCE: This research result has demonstrated that the endoparasitic nematophagous fungus, E. vermicola, mimics the scent of PWN host pine tree to entice PWN for the nutrient. The identification of the attractive VOCs emitted from the fungus E. vermicola is of significance in better understanding parasitic mechanism of the fungus and the co-evolution in the two organisms and will aid management of the pine wilt disease.
Subject(s)
Ascomycota/metabolism , Chemotactic Factors/metabolism , Tylenchida/microbiology , Volatile Organic Compounds/metabolism , Animals , Ascomycota/chemistry , Ascomycota/physiology , Bicyclic Monoterpenes , Bridged Bicyclo Compounds/chemistry , Bridged Bicyclo Compounds/metabolism , Camphor/chemistry , Camphor/metabolism , Chemotactic Factors/chemistry , Gas Chromatography-Mass Spectrometry , Host-Parasite Interactions , Host-Pathogen Interactions , Monoterpenes/chemistry , Monoterpenes/metabolism , Mycelium/chemistry , Mycelium/metabolism , Mycelium/physiology , Odorants , Pinus/microbiology , Pinus/parasitology , Plant Diseases/microbiology , Plant Diseases/parasitology , Tylenchida/physiology , Volatile Organic Compounds/chemistry , Wood/microbiology , Wood/parasitologyABSTRACT
A cDNA encoding cysteine protease inhibitor (CPI) was isolated from the cDNA library of clamworm Perinereis aibuhitensis Grube. The deduced amino acid sequence analysis showed that the protein had 51%, 48%, and 48% identity with Zgc:153129 from Danio rerio, cystatin B from Theromyzon tessulatum and ChainA, stefin B tetramer from Homo sapiens, respectively. The gene was cloned into the intracellular expression vector pET-15b and expressed in Escherichia coli. The recombinant CPI (PA-CPI) was purified by affinity chromatography on Ni-charged resin and ion-exchange chromatography on DEAE-Sepharose FF. The relative molecular mass of PA-CPI was 16 KDa deduced by SDS-PAGE. Activity analysis showed that the recombinant protein could inhibit the proteolytic activity of papain. A constitutive and secretive expression vector was also constructed, and the cDNA encoding CPI was subcloned into the vector for extracellular expression. Western blotting analysis results showed that the PA-CPI was secreted into the medium. Bioassay demonstrated that E. coli DH5alpha harboring pUC18ompAcat-CPI showed a significant difference in mortality to the Asian longhorned beetle Anoplophora glabripennis compared with untransformed E. coli DH5alpha and control.
