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Production, purification and characterization of an extracellular keratinase from Lysobacter NCIMB 9497
Author(s) -
Allpress J.D.,
Mountain G.,
Gowland P.C.
Publication year - 2002
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1046/j.1472-765x.2002.01093.x
Subject(s) - keratinase , pmsf , proteases , bacteria , phenylmethylsulfonyl fluoride , extracellular , microbiology and biotechnology , biology , protease , metalloproteinase , biochemistry , enzyme , chemistry , genetics
Aims: The aim of this study was to determine the keratinolytic ability of a range of bacteria and subsequently, to characterize the keratinase showing the greatest biotechnological potential. Methods and Results: Nine bacteria, reported to produce extracellular proteases, were screened for production of keratinases. Of these, Lysobacter NCIMB 9497 exhibited the highest keratinolytic activity. The keratinase from this strain (M r 148 kDa) was purified and characterized. Optimum activity occurred at 50°C; no inhibition was demonstrated by phenylmethylsulphonyl fluoride (PMSF), but inhibition by EDTA was demonstrated. Conclusions: This study indicates that keratinase is a metalloprotease with a high degree of keratinolytic activity and stability. Significance and Impact of the Study: This is the first detailed report of a metalloprotease with keratinolytic activity. The novel reaction mechanism, degree of keratinolytic activity and stability indicate considerable biotechnological potential in the leather industry, and in the processing of poultry waste.