new thermostable serine keratinase produced by thermoactive and brevibacilus brevis strain us575 industrial interest in the biodegradation of keratin substrates and high enzyme unhairing in leather processing

摘要

the present invention relates to the purification to homogeneity of a new extracellular keratinase as kerus produced from brevibacillus brevis strain us575 and molecular and biochemical characterization of this enzyme. the size of the kerus keratinase was estimated by sds-page to 29kda. the optimum activity was obtained at ph 8 and 40.it is an enzyme belonging to the family of serine proteases in the fact that it is inhibited by pmsf and dfp, essentially. characterization of keratinase kerus and considerably improved by calcium.characterization of keratinase kerus and comparative study with two enzymes currently used in river operations during the processing of leather tanning naked 12 mg (for stage of depilation and koroponu00ae mk eg during bating) show that the ke ratinase kerus is characterized by an important thermostability.a broad specificity and catalytic efficiency of a substrate. we have shown that the kerus may have use in the treatment of leather, especially during the process of enzymatic dehairing dehairing because it shows a remarkable level of raw hides and skins of rabbit, goat, cow and sheep.we investigated the potential of brevibacillus brevis us575 keratinolytic strain on various substrates (rich in keratin from poultry feathers feather meal, poultry, whole, rabbit hair, goat hair.hair from cows and sheep wool), and the performance of the native enzyme and the enzyme enzyme unhairing operation key step in leather processing.this study has shown that the us575 brevibacillus brevis strain and its enzyme (kerus) are keratinolytic activity seems to be an interesting and can be used with success in biotechnology applications, such as leather processing, since it meets the requirements these excellent keratinase in tanning.