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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 also increased (109.9–119%) with increasing concentration of urea (2–8 mole/l). The enzyme was identified...
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