alexa Characterization of a keratinolytic serine proteinase from Streptomyces pactum DSM 40530.
Chemical Engineering

Chemical Engineering

Journal of Bioprocessing & Biotechniques

Author(s): Bckle B, Galunsky B, Mller R

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Abstract A serine protease from the keratin-degrading Streptomyces pactum DSM 40530 was purified by casein agarose affinity chromatography. The enzyme had a molecular weight of 30,000 and an isoelectric point of 8.5. The proteinase was optimally active in the pH range from 7 to 10 and at temperatures from 40 to 75 degrees C. The enzyme was specific for arginine and lysine at the P1 site and for phenylalanine and arginine at the P1' site. It showed a high stereoselectivity and secondary specificity with different synthetic substrates. The keratinolytic activity of the purified proteinase was examined by incubation with the insoluble substrates keratin azure, feather meal, and native and autoclaved chicken feather downs. The S. pactum proteinase was significantly more active than the various commercially available proteinases. After incubation with the purified proteinase, a rapid disintegration of whole feathers was observed. But even after several days of incubation with repeated addition of enzymes, less than 10\% of the native keratin substrate was solubilized. In the presence of dithiothreitol, degradation was more than 70\%.
This article was published in Appl Environ Microbiol and referenced in Journal of Bioprocessing & Biotechniques

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