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 ยฐC. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a
Purification and characterization of a protease from jackfruit latex
โ Scribed by K.M. Renuka Prasad; Tumkur K. Virupaksha
- Publisher
- Elsevier Science
- Year
- 1990
- Tongue
- English
- Weight
- 372 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0031-9422
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