Back to Search
Start Over
Keratinolytic activity of purified alkaline keratinase produced by Scopulariopsis brevicaulis (Sacc.) and its amino acids profile
- Source :
- Saudi Journal of Biological Sciences. 18(2):117-121
- Publication Year :
- 2011
- Publisher :
- Elsevier BV, 2011.
-
Abstract
- Sodium dodecyl sulfate–polyacrlyamide gel electrophoresis (SDS–PAGE) was used to assess the purity and molecular weight of the previously purified alkaline keratinase enzyme of Scopulariopsis brevicaulis. The enzyme was homogenous, as seen by a single band of protein, and had an apparent molecular weight of 28.5kDa. Amino acid profile of the purified keratinase revealed that it was composed of 14 different amino acids with high proportions of glutamic acid (20.86%), alanine (14.52%), glycine (14.21%), leucine (8.59%) and serine (7.81%). The enzyme contained moderate amounts of valine (6.01%), threonine (5.58%) and phenyl alanine (5.22%). The purified enzyme of S. brevicaulis exerted a potent keratinolytic activity and was capable to hydrolyze different keratinaceous materials with highest activity on chicken feathers followed by human nails and human hair.
- Subjects :
- Gel electrophoresis
Alanine
chemistry.chemical_classification
biology
Keratinase
Agricultural and Biological Sciences(all)
Fungi
Keratinolytic activity
Amino acid
chemistry
Biochemistry
Valine
SDS–PAGE
Glycine
biology.protein
Keratinaceous materials
Amino acids
Original Article
Leucine
General Agricultural and Biological Sciences
Polyacrylamide gel electrophoresis
GeneralLiterature_REFERENCE(e.g.,dictionaries,encyclopedias,glossaries)
ComputingMilieux_MISCELLANEOUS
Subjects
Details
- ISSN :
- 1319562X
- Volume :
- 18
- Issue :
- 2
- Database :
- OpenAIRE
- Journal :
- Saudi Journal of Biological Sciences
- Accession number :
- edsair.doi.dedup.....11c35d58103d9256520f1b74c7e1d611
- Full Text :
- https://doi.org/10.1016/j.sjbs.2010.12.011