Effect of pyrolysis temperature and molecular weight on characterization of biochar derived dissolved organic matter from invasive plant and binding behavior with the selected pharmaceuticals.

A comprehensive understanding of the characteristics of biochar released-dissolved organic matter (BDOM) derived from an invasive plant and its impact on the binding behavior of pharmaceuticals is essential for the application of biochar, yet has received less attention. In this study, the binding behavior of BDOM pyrolyzed at 300-700 °C with sulfathiazole, acetaminophen, chloramphenicol (CAP), and carbamazepine (CMZ) was investigated based on a multi-analytical approach. Generally, the pyrolysis temperature exhibited a more significant impact on the spectral properties of BDOM and pharmaceutical binding behavior than those of the molecular weight. With increased pyrolysis temperature, the dissolved organic carbon decreased while the proportion of the protein-like substance increased. The highest binding capacity towards the drugs was observed for the BDOM pyrolyzed at 500 °C with the molecular weight larger than 0.3 kDa. Moreover, the protein-like substance exhibited higher susceptive and released preferentially during the dialysis process and also showed more sensitivity and bound precedingly with the pharmaceuticals. The active binding points were the aliphatic C-OH, amide II N-H, carboxyl CO, and phenolic-OH on the tryptophan-like substance. Furthermore, the binding affinity of the BDOM pyrolyzed at 500 °C was relatively high with the stability constant (logKM) of 4.51 ± 0.52.

Characterization of copper binding to biochar-derived dissolved organic matter: Effects of pyrolysis temperature and natural wetland plants.

Characterization of the biochar-derived dissolved organic matter (BDOM) is essential to understanding the environmental efficacy of biochar and the behavior of heavy metals. In this study, the binding properties of BDOM derived from different pyrolysis temperatures, wetland plants, and plant organs with Cu was investigated based on a multi-analytical approach. In general, the pyrolysis temperature exhibited a more significant impact on both the spectral characteristics of BDOM and Cu binding behavior than those of the feedstocks. With the pyrolysis temperature increased, the dissolved organic carbon, aromaticity, and fluorescence substance of BDOM decreased and the structure became more condensed. Humic-and tryptophan-like substance was more susceptible to the addition of Cu for BDOM pyrolyzed at 300 â„ƒ and 500 â„ƒ, respectively. In addition, the more tyrosine-like substance is involved in Cu binding at higher pyrolysis temperature (500 â„ƒ). However, the fluvic-like substance occurred preferentially with Cu than the other fluorophores. Moreover, the higher binding capacity for Cu was exhibited by the humic-like substance and by BDOM derived from the higher pyrolysis temperature and the lower elevation plants with the corresponding average stability constants (log KM) of 5.58, 5.36, and 5.16.

Purification and characterization of alpha-mucrofibrase, a novel serine protease with alpha-fibrinogenase activity from the venom of Chinese Habu (Trimeresurus mucrosquamatus).

A novel fibrinogenolytic protease, named alpha-mucrofibrase, was purified from the venom of Chinese Habu (Trimeresurus mucrosquamatus) by DEAE-Sephadex A-50 ion-exchange chromatography and Sephadex G-100 (super fine) gel filtration alpha-Mucrofibrase is a single-chain polypeptide of approximately 29 kDa. It is stable even at 95 degrees C, and the most susceptible hydrolysis substrate is S-2302. It cleaved primarily the Aalpha chain of fibrinogen followed by the Bbeta chain, while the gamma chain was partially affected. N-terminal sequence of this fibrinogenolytic enzyme has great homology with those of other snake venom serine proteases. The esterase activity of alpha-mucrofibrase is inhibited by phenylmethylsulfonyl fluoride (PMSF) but not by metal chelator (EDTA), suggesting this fibrinogenase belongs to the venom serine protease family.