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Purification and characterization of a levanase from Streptomyces sp. 366L

โœ Scribed by Young Soon Lim; Soo Kyung Kang; Sang Ok Lee; Jae Dong Lee; Tae Ho Lee


Book ID
119524893
Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
144 KB
Volume
61
Category
Article
ISSN
0168-1656

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