Purification and characterization of an alkaline keratinase from Streptomyces sp.
A protease producing bacterial culture ('S7') was isolated from slaughterhouse waste samples, Hyderabad, India. It was related to Streptomyces sp. on the basis of biochemical properties and 16S rRNA gene sequencing. Purification of the protease present in the culture medium supernatant on sephacryl S-100 indicated that it contains a keratinase with 67% recovery, 2.5-fold purification and an estimated molecular mass of approximately 44,000 Da. Keratinase showed an optimal activity at 45 degrees C and pH 11. Keratinase activity increased substantially in presence of Ca(2+) and was inhibited in presence of PMSF and EDTA identifying it as a serine metalloprotease. Stability in the presence of detergents, surfactants and solvents make this keratinase extremely useful for biotechnological process involving keratin hydrolysis or in the leather industry.
Tatineni
Radhika
R
Center for Biotechnology, Institute of Science and Technology, JNT University, Hyderabad, India.
Doddapaneni
Kiran Kumar
KK
Potumarthi
Ravi Chandra
RC
Vellanki
Ravi Nagaraj
RN
Kandathil
Manjusha Thomas
MT
Kolli
Nilima
N
Mangamoori
Lakshmi Narasu
LN
D000180:Acrylic Resins / Q000737:chemistry; D000818:Animals; D001709:Biotechnology / Q000379:methods*; D002118:Calcium / Q000737:chemistry; D002645:Chickens; D004492:Edetic Acid / Q000737:chemistry; D005241:Feathers; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007633:Keratins / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry* / Q000302:isolation & purification*; D012336:RNA, Ribosomal, 16S / Q000737:chemistry; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature