Physicochemical Properties of the Native, Zinc- and Manganese-Prepared Metalloprotease of Bacillus polymyxa
AUTOR(ES)
Griffin, Patrick J.
RESUMO
The neutral protease of Bacillus polymyxa had a broad pH optimum (6.0 to 7.2) for activity at 37 C. The enzyme was most stable at pH 5.6 to 5.8. The protease had an optimum temperature of 37 C and was quite thermostable up to 35 C, but at higher temperatures the stability decreased rapidly. The substrate specificity of the protease was similar to that of the neutral proteases of other members of the genus Bacillus. The enzyme was shown to be a zinc metalloprotease. However, manganous ions had a greater activating and stabilizing influence on the activity of this enzyme than zinc. Replacement of zinc in the native enzyme by manganese resulted in a 50% increase in activity. In addition, the prepared manganese metalloprotease had higher temperature and more alkaline pH optima than the native enzyme.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=379749Documentos Relacionados
- Production and Purification of the Metalloprotease of Bacillus polymyxa
- Preparation and Properties of the Amylases Produced by Bacillus macerans and Bacillus polymyxa1
- Physicochemical, thermal and rheological properties of three native corn starches
- Photoaffinity labeling of the gonadotropin receptor with native, asialo, and deglycosylated choriogonadotropin.
- Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis.