An extracellular alkaline serine protease has been purified from Aspergillus terreus (IJIRA 6.2). The purification procedure involved chromatography on DEAE-Sephadex A25, phosphocellulose, hydroxyapatite, casein-Sepharose, gel filtration on Sephacryl-S-300 and by glycerol density gradient centrifugation. The enzyme was further purified to apparent homogeneity through a combination of electrophoresis in polyacrylamide gel containing 0.1% sodium dodecyl sulfate (SDS) with or without protease substrate (gelatin) and subsequent regeneration of its activity in situ by removal of SDS. The active enzyme was visualized in a zymogram or on the basis of protease activity exhibited on an X-ray film. The protein in the unstained segment of the gel was electroeluted. The eluted protein with protease activity exhibited a molecular mass of 37,000-daltons on electrophoresis in SDS-polyacrylamide gel. A sedimentation coefficient of 3.2S was obtained by glycerol density gradient contrifugation. Maximum activity of protease was observed at pH 8.5 and at 37 degrees C. Purified protease was active between pH 5.5 and 9.5 and was found to be stable up to 60 degrees C. With Na-caseinate, the K(m) of the purified protease was found to be 0.055 mM. Antipain, phenylmethane sulfonyl fluoride, and chymostatin served as non-competitive inhibitors. Substrate specificity was determined by using a synthetic chromogenic peptide containing N-P-Tosyl-Gly-Pro-Arg-p-nitroanilide. Results showed that the protease cleaved the peptide on the -COOH end of arginine residue.
Three novel water soluble neutral mononuclear oxidovanadium(iv) complexes 1-3, [VOLB] (where HL = dipicolinic acid (DPA) and B = imidazole (1)/1-methylimidazole (2)/1-allylimidazole (3)), were synthesized by the reaction of [VOL(HO)] with imidazole/1-methylimidazole/1-allylimidazole in ethanol. The complexes were thoroughly characterized by elemental analysis, IR, UV-Vis and EPR spectroscopy, magnetic susceptibility, cyclic voltammetry and single crystal X-ray diffraction techniques. In all the complexes the vanadium(iv) centre assumes a distorted octahedral environment. All the three complexes have similar structures and contain a range of intramolecular interactions such as hydrogen bonding, C-Hπ, and ππ stacking dominating their supramolecular architectures. A thermal study of the complexes was carried out to analyze their stability. The energy of non-covalent interactions and frontier orbitals for the complexes were also calculated by DFT. In order to investigate the binding interactions and conformational changes of the secondary structure of bovine serum albumin (BSA) with the complexes, absorption, fluorimetric titration and circular dichroism measurements in aqueous medium were carried out. Molecular docking studies have also been carried out to understand the binding modes and interaction patterns of the oxidovanadium(iv) complexes with BSA. The anticancer activities of the ligand and complexes 1-3 were tested against the human hepatic carcinoma cell line Hep3B. The complexes showed prominent cytotoxicity towards cancer cells.
The brightness of peroxide bleached jute material increased by about 3% when pretreated with an enzyme mix containing cellulase and xylanase. Pretreatment for 6 hours at pH 5.0 and 45°C using 0.2 u (unit) cellulase and 2.6 u of xylanase per gram of fibers gave the best results. Additives like nonionic surfactants or chelating agents during pretreatment further enhanced the brightness. Pretreatment reduced the per oxide requirement for bleaching and rendered the jute materials distinctly softer.
Recently, a new phytoplasma was discovered in Hillsborough County in the state of Florida, USA. This phytoplasma belongs to the 16SrIV taxonomic group and is classified as subgroup D. It is the causal agent of lethal bronzing disease (LBD) of palm. Since the discovery of LBD in 2006, the disease has spread throughout much of the state. In 2014 and 2015, stands of cabbage palm and queen palms that had been present at the University of Florida's Fort Lauderdale Research and Education Center in Davie, FL began showing symptoms of LBD. After confirming the presence of the LBD phytoplasma in initially infected palms by nested PCR and RFLP analysis, all palms were systematically sampled over the period of 1 year to monitor and quantify disease spread. A total of 30 cabbage palms were tested monthly by qPCR, with five testing positive on the first sample date. By the end of the study period, 16 cabbage palms had died from the infection. A total of 16 queen palms were surveyed, with three palms initially testing positive. By the end of the study, four queen palms had tested positive and died from the infection. To the authors' knowledge, this study is the first to document and quantify spread of palm-infecting phytoplasmas. This data provides important insights into the ecology of palm-infecting phytoplasmas and highlights the impact that the movement of infective insects can pose to established stands of palms.
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