Production, characterization and application of keratinase from Streptomyces gulbargensis.
A Streptomyces gulbargensis newly isolated, thermotolerant feather-degrading bacterial strain was investigated for its ability to produce keratinase enzyme. Maximum keratinolytic activity was observed at 45 degrees C and pH 9.0 at 120 h of incubation. Activity was completely stable (100%) between 30 and 45 degrees C and pH 7.0-9.0, respectively. Addition of starch to the growth medium affects the activity by means of increase in keratinase secretion. After seven days of cultivation, 10-fold increase (14.3 U ml(-1)) in keratinase activity was observed in the presence of 3g starch (per liter) of the medium. The enzyme was monomeric and had a molecular mass of 46 kDa. The enzyme activity was significantly inhibited by CaCl(2) and partly inhibited by EDTA, whereas, Na(2)SO(3) enhance the enzyme activity by 2.9 times more. In addition, native chicken feather was completely degraded at 96 h of incubation. The results obtained showed that newly isolated strain S. gulbargensis could be a useful in biotechnology in terms of valorization of keratin-containing wastes or in the leather industry.
Syed
Dastager G
DG
National Institute of Interdisciplinary Science and Technology CSIR, Thiruvananthapuram, India. syedmicro@gmail.com
Lee
Jae Chan
JC
Li
Wen-Jun
WJ
Kim
Chang-Jin
CJ
Agasar
Dayanand
D
D000645:Ammonium Sulfate / Q000378:metabolism; D000818:Animals; D019149:Bioreactors; D001709:Biotechnology / Q000379:methods*; D004587:Electrophoresis, Agar Gel; D005241:Feathers / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D010447:Peptide Hydrolases / Q000096:biosynthesis*; D011200:Poultry; D013213:Starch; D013302:Streptomyces / Q000201:enzymology*; D013696:Temperature; D013997:Time Factors
D013213:Starch; D010447:Peptide Hydrolases; C035855:keratinase; D000645:Ammonium Sulfate