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Purification and characterization of a novel protease from culture filtrates of a Streptomyces sp.

✍ Scribed by Françoise Bono; Pierre Savi; Anne Tuong; Mohamed Maftouh; Jean-Marie Pereillo; Joel Capdevielle; Jean-Claude Guillemot; Jean-Pierre Maffrand; Jean-Marc Herbert


Book ID
116131995
Publisher
John Wiley and Sons
Year
1996
Tongue
English
Weight
606 KB
Volume
141
Category
Article
ISSN
0378-1097

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A 20 kDa antifungal serine protease from Streptomyces sp. A6 was purified to 34.56 folds by gel permeation chromatography. The enzyme exhibited highest activity at neutral to near alka- line pH 7-9 and 55 °C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a