Search results for "Laccases"
showing 3 items of 3 documents
Anticancer, antioxidant, and antibacterial activities of low molecular weight bioactive subfractions isolated from cultures of wood degrading fungus …
2017
The aim of this study is to investigate in vitro the anticancer, antioxidant, and antibacterial activities of three low molecular weight subfractions I, II and III isolated from secondary metabolites produced by the wood degrading fungus Cerrena unicolor. The present study demonstrated that the low molecular weight subfractions III exhibited the strongest inhibitory activity towards breast carcinoma cells MDA-MB-231, prostatic carcinoma cells PC3, and breast cancer cells MCF7 with the half-maximal inhibitory concentration (IC50) value of 52,25 μg/mL, 60,66 μg/mL, and 54,92 μg/mL, respectively. The highest percentage of inhibition was noted at a concentration of 300 μg/mL in all the examined…
First extensive characterization of the venom gland from an egg parasitoid: structure, transcriptome and functional role.
2018
The venom gland is a ubiquitous organ in Hymenoptera. In insect parasitoids, the venom gland has been shown to have multiple functions including regulation of host immune response, host paralysis, host castration and developmental alteration. However, the role played by the venom gland has been mainly studied in parasitoids developing in larval or pupal hosts while little is known for parasitoids developing in insect eggs. We conducted the first extensive characterization of the venom of the endoparasitoid Ooencyrtus telenomicida (Vassiliev), a species that develops in eggs of the stink bug Nezara viridula (L.). In particular we investigated the structure of the venom apparatus, its functio…
Recombinant laccase from Pediococcus acidilactici CECT 5930 with ability to degrade tyramine
2017
Biogenic amines degradation by bacterial laccases is little known, so we have cloned and heterologously expressed, in E. coli, a new laccase from Pediococcus acidilactici CECT 5930 (Lpa5930), a lactic acid bacterium commonly found in foods able to degrade tyramine. The recombinant enzyme has been characterized by physical and biochemical assays. Here we report the optimization of expression and purification procedures of this laccase. DNA encoding sequence of laccase from P. acidilactici was amplified by PCR and cloned into the expression plasmid pET28a for induction by isopropyl-β-D-thiogalactoipyranoside. Protein expression was performed in E. coli BL21(DE3) harboring pGro7 plasmid expres…