Purification and characterization of a keratinolytic metalloprotease from Chryseobacterium sp. kr6
✍ Scribed by Alessandro Riffel; Adriano Brandelli; Cláudia de M. Bellato; Gustavo H.M.F. Souza; Marcos N. Eberlin; Flavio C.A. Tavares
- Book ID
- 118471835
- Publisher
- Elsevier Science
- Year
- 2007
- Tongue
- English
- Weight
- 467 KB
- Volume
- 128
- Category
- Article
- ISSN
- 0168-1656
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract **BACKGROUND:** Keratinases are important enzymes for biotechnological processes involving keratin hydrolysis. In this work substrate specificity and kinetic properties of a keratinase from __Chryseobaterium__ sp. were investigated. **RESULTS:** The optimal conditions for activity of p
A 20 kDa antifungal serine protease from Streptomyces sp. A6 was purified to 34.56 folds by gel permeation chromatography. The enzyme exhibited highest activity at neutral to near alka- line pH 7-9 and 55 °C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a