We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Purification and characterization of an efficient poultry feather degrading-protease from Myrothecium verrucaria.
- Authors
Moreira-Gasparin, Fabiana G.; de Souza, Cristina G. Marques; Costa, Andréa M.; Alexandrino, Ana Maria; Bracht, Cissa K.; Boer, Cinthia G.; Peralta, Rosane M.
- Abstract
The purpose of this work was to characterize an alkaline protease from the filamentous fungus Myrothecium verrucaria and to explore its capability to degrade native poultry feathers. The enzyme was purified to homogeneity using a single chromatographic step. Recovery was high, 62%, with a specific activity of 12,851.8 U/mg protein. The enzyme is a small monomeric protein with a molecular mass of 22 ± 1.5 kDa. It presented pH optimum of 8.3 and was stable over a broad pH range (5.0-12.0). The temperature optimum was 37°C, with thermal stability at temperatures up to 45°C. The enzyme presented an efficiency of 80.3% in the degradation of poultry feather meal, releasing amino acids and soluble peptides. It was able to hydrolyze β-keratin without necessity of chemical or enzymatic reduction of the disulphide bonds. Considering that, everyday, poultry-processing plants produce feathers as a waste products, this protease can be useful in biotechnological processes aiming to improve the transformation of poultry feathers through solubilization of β-keratin into usable peptides. Furthermore, it can also be useful in processes aiming to reduce the environmental pollution caused by the accumulation of feathers.
- Subjects
MYROTHECIUM verrucaria; BIODEGRADATION; AMINO acids; SEWAGE purification by-products; WASTE products; BIOTECHNOLOGICAL process control; BIOACCUMULATION
- Publication
Biodegradation, 2009, Vol 20, Issue 5, p727
- ISSN
0923-9820
- Publication type
Article
- DOI
10.1007/s10532-009-9260-4