Production and characterization of keratinase of a feather-degrading Bacillus licheniformis PWD-1.
The keratinase produced by Bacillus licheniformis PWD-1 was induced by feather powder. Maximal enzyme production could be achieved by culturing in a medium containing 1% hammer-milled feather powder (100 mesh) at 45 degrees C for 30 h. Maximal growth of PWD-1 was achieved at 50 degrees C, and maximal enzyme induction was at 45 degrees C. The molecular mass and isoelectric point of this enzyme were 31.4 kDa and 8.5, respectively. This enzyme was stable from pH 5 to 12. The optimal reaction pHs for feather powder and casein were 8.5 and 10.5 to 11.5, respectively. The optimal reaction temperature was 50 degrees C to 55 degrees C. The relative activity of this enzyme toward casein, feather powder, keratin, elastin, and collagen was 100:52:41:18:7, and 100:56:32:3 for Suc-AAPL-pNA, Suc-AAPF-pNA, Suc-AAPM-pNA, and Suc-AAVA-pNA (Suc, succinyl; pNA, p-nitrophenylanilide).
Cheng
S W
SW
Institute of Biochemistry, National Yang-Ming University, Taipei, Taiwan, Republic of China.
Hu
H M
HM
Shen
S W
SW
Takagi
H
H
Asano
M
M
Tsai
Y C
YC
D000595:Amino Acid Sequence; D000818:Animals; D001407:Bacillus / Q000201:enzymology*; D001431:Bacteriological Techniques; D002645:Chickens; D005241:Feathers / Q000378:metabolism*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007231:Infant, Newborn; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000096:biosynthesis* / Q000378:metabolism; D013696:Temperature
D010447:Peptide Hydrolases; C035855:keratinase