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Purification and characterization of xylanases from Streptomyces spp. SWU 10

✍ Scribed by W. Sukhumsirichart; W. Deesukon; T. Sakamoto

Publisher
Elsevier
Year
2009
Tongue
English
Weight
91 KB
Volume
25
Category
Article
ISSN
1871-6784

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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 Β°C. Neutral surfactant triton X-100 enhanced the activity by 4.12 fold. The protease activity a