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Production and properties of keratinolytic proteases from three novel Gram-negative feather-degrading bacteria isolated from Brazilian soils.
- Source :
-
Biodegradation [Biodegradation] 2011 Nov; Vol. 22 (6), pp. 1191-201. Date of Electronic Publication: 2011 Apr 28. - Publication Year :
- 2011
-
Abstract
- The keratinolytic potential and protease properties of three novel Gram-negative feather-degrading bacteria isolated from Brazilian soils was described. Aeromonas hydrophila K12, Chryseobacterium indologenes A22 and Serratia marcescens P3 were able to degrade feather meal, producing high amounts of soluble proteins and forming thiol groups. The proteases of strains K12, A22 and P3 had optimal pH of 8.0, 7.5 and 6.0, respectively; this last is an uncommon feature for bacterial keratinases. The optimal temperature was in the range 45-55°C. All three proteases were active towards azokeratin and were inhibited by EDTA, suggesting that they are keratinolytic metalloproteases. The proteolytic activity of K12 was stimulated by organic solvents and the detergent SDS, suggesting its potential application for detergent formulations and peptide synthesis. Strains A22, K12 and P3 have great potential for use in biotechnological processes involving hydrolysis of keratinous byproducts.
- Subjects :
- Animals
Brazil
Culture Media
Edetic Acid pharmacology
Feathers chemistry
Hydrogen-Ion Concentration
Hydrolysis drug effects
Poultry
Sodium Dodecyl Sulfate pharmacology
Soil
Soil Microbiology
Substrate Specificity
Temperature
Waste Products
Aeromonas hydrophila enzymology
Bacterial Proteins metabolism
Biodegradation, Environmental
Chryseobacterium enzymology
Feathers metabolism
Industrial Microbiology methods
Keratins metabolism
Peptide Hydrolases metabolism
Serratia marcescens enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1572-9729
- Volume :
- 22
- Issue :
- 6
- Database :
- MEDLINE
- Journal :
- Biodegradation
- Publication Type :
- Academic Journal
- Accession number :
- 21526391
- Full Text :
- https://doi.org/10.1007/s10532-011-9474-0