Article Abstract:
A culture of Streptomyces retuculi with mycelium-associated cellulolytic activity was grown in the presence of Avicel to isolate and purify the Avicelase enzyme. The enzyme was purified to homogeneity by two consecutive anion-exchange chromatographies followed by chromatofocusing. The purified enzyme was an 82-kDa cellulase which could degrade crystalline and soluble cellulose as well as cellodextrins and p-nitrophenylcellobioside. Protease treatment yielded a 42-kDa truncated form which retained its cellulolytic activities.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
The purification and biochemical characterization of the protease which is responsible for the modification of the Streptomyces reticuli cellulase (Avicelase) Cel-1 were presented. The highest activity of the 36-kDa protease was determined at 55 degrees C and between pH 7.0 and 7.7. It was able to hydrolyze gelatin and the chromogenic substrates Azocoll, Azocasein and Azoalbumin. Additional studies suggest that this enzyme is not covalently glycosylated.
User Contributions:
Comment about this article or add new information about this topic:
Article Abstract:
A study was conducted on the regulation of Avecilase, Cel1 synthesis regulation. Only the carbon source crystalline cellulose was found to trigger Avicelase synthesis. Comparative media studies with low and high buffering capacities showed that low hydrogen-ion concentration represses Avicelase synthesis. Glucose kinase was proven to be inessential for the repression effect.
User Contributions:
Comment about this article or add new information about this topic: