Keratin degradation: a cooperative action of two enzymes from Stenotrophomonas sp.
A novel keratin-degrading bacterium Stenotrophomonas sp. strain D-1, isolated from deer fur, produced two types of extracellular proteins: proteolytic and disulfide bond-reducing. The results on the biochemical properties suggest that this protease belongs to the serine protease, and the disulfide bond-reducing protein could be the disulfide reductase type. None of these enzymes showed keratinolytic activity independently. However, after mixing of the two enzymes, the keratinolytic activity was increased tremendously (more than 50-fold) over that of the protease only. This keratinolytic activity was more than 2-fold higher than that of the combination with proteinase K (also known for its high keratinolytic activity). Since the two enzymes discovered in this study acted cooperatively and resulted in higher keratinolytic activity, a new mechanism of keratin degradation has been revealed. To our knowledge, this is the first report on the cooperative action of two enzymes resulting in the effective degradation of keratin.
Yamamura
Shohei
S
School of Materials Science, Japan Advanced Institute of Science and Technology, 1-1 Asahidai, Tatsunokuchi, Ishikawa 923-1292, Japan.
Morita
Yasutaka
Y
Hasan
Quamrul
Q
Yokoyama
Kenji
K
Tamiya
Eiichi
E
D001426:Bacterial Proteins / Q000302:isolation & purification / Q000378:metabolism; D004220:Disulfides / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D007633:Keratins / Q000378:metabolism*; D007700:Kinetics; D008956:Models, Chemical; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D020588:Stenotrophomonas / Q000201:enzymology*; D013379:Substrate Specificity
D001426:Bacterial Proteins; D004220:Disulfides; D007633:Keratins; D010088:Oxidoreductases; D012697:Serine Endopeptidases