Project description:Cellulophaga lytica (Lewin 1969) Johansen et al. 1999 is the type species of the genus Cellulophaga, which belongs to the family Flavobacteriaceae within the phylum 'Bacteroidetes' and was isolated from marine beach mud in Limon, Costa Rica. The species is of biotechnological interest because its members produce a wide range of extracellular enzymes capable of degrading proteins and polysaccharides. After the genome sequence of Cellulophaga algicola this is the second completed genome sequence of a member of the genus Cellulophaga. The 3,765,936 bp long genome with its 3,303 protein-coding and 55 RNA genes consists of one circular chromosome and is a part of the Genomic Encyclopedia of Bacteria and Archaea project.
Project description:Genome-wide transcriptomics (RNA-seq) data was obtained temporally at 0, 15, 30, 45, 60 and 120 minutes of the infection with phage 18:3 on Cellulophaga baltica strain #18 to analyze, in biological triplicates, the phage and host transcriptional response during their interaction compared to the uninfected control.
Project description:A carrageenan-degrading marine Cellulophaga lytica strain N5-2 was isolated from the sediment of carrageenan production base. A ?-carrageenase (EC 3.2.1.83) with high activity was purified to electrophoretic homogeneity from the culture supernatant by a procedure of ammonium sulfate precipitation, dialyzing and gel filtration on SephadexG-200 and SephadexG-75. The purified enzyme was verified as a single protein on SDS-PAGE, and whose molecular weight was 40.8 kDa. The ?-carrageenase yielded a high activity of 1170 U/mg protein. For ?-carrageenase activity, the optimum temperature and pH were 35 °C and pH 7.0, respectively. The enzyme was stable at 40 °C for at least 2.5 h. The enzyme against ?-carrageenan gave a Km value of 1.647 mg/mL and a Vmax value of 8.7 ?mol/min/mg when the reaction was carried out at 35 °C and pH 7.0. The degradation products of the k-carrageenase were analyzed by thin layer chromatography (TLC), high performance liquid chromatography (HPLC), electrospray ionization time-of-flight mass spectroscopy (ESI-TOF-MS) and 13C-NMR spectroscopy, and the results indicated that the enzyme was specific of the ?-1,4 linkage and hydrolyzed ?-carrageenan into ?-neocarraoctaose-sulfate and ?-neocarrahexaose-sulfate first, and then broke ?-neocarraoctaose-sulfate into ?-neocarrabiose-sulfate and ?-neocarrahexaose-sulfate.