RESUMO
A novel cellulase was isolated from the thermoacidophilic bacterium Alicyclobacillus acidocaldarius ATCC27009 grown in medium containing carboxymethylcellulose. The enzyme is a glycosylated monomer of 56.2 kDa, relatively thermostable, with optimal pH and temperature of 4.0 and 65 degrees C, respectively. Enzymatic assays on several polysaccharides demonstrated that CelG was specific for carboxymethylcellulose.
Assuntos
Celulase/química , Celulase/isolamento & purificação , Bactérias Gram-Positivas Formadoras de Endosporo/enzimologia , Celulase/metabolismo , Cromatografia de Afinidade , Cromatografia em Gel , Eletroforese em Gel de Poliacrilamida , Concentração de Íons de Hidrogênio , Especificidade por Substrato , Temperatura , UltracentrifugaçãoRESUMO
A bacterium which can grow on chicken feathers and which exhibits keratinolytic activity was isolated from solfataric muds. It was classified as belonging to the genus Clostridium and closely related to C. sporogenes. Based on its unique capability to degrade chicken feathers, it was designated as Clostridium sporogenes bv. pennavorans bv. nov. The keratinase purified from the culture supernatant is a monomer of 28.7kDa molecular mass. The enzyme is relatively thermostable and is active over a broad range of temperature and pH. Specific enzymatic assays demonstrate that keratinase can act on a large variety of soluble and insoluble protein substrates.
