An extracellular protease of the micromycete Alternaria alternataстатья
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Дата последнего поиска статьи во внешних источниках: 7 октября 2013 г.
Местоположение издательства:Road Town, United Kingdom
Первая страница:1350
Последняя страница:1354
Аннотация:An extracellular protease was isolated from the mycelial fungus Alternaria alternata. The enzyme was purified 1300-fold with a yield of 8.3% by affinity chromatography and gel filtration. The molecular weight of the purified protease is 33 kD. The enzyme is maximally active at 48°C and pH 8.0 and 9.1 with BAPA and casein as substrates, respectively, is stable below 30°C, and rapidly loses activity at higher temperature. Based on its inhibitor sensitivity, the extracellular protease of A. alternata can be classified as a serine protease. The substrate specificity of the enzyme is characteristic of trypsin-like proteases.