Characterization of an extracellular alkaline serine protease from marine Engyodontium album BTMFS10
نویسندگان
چکیده
منابع مشابه
Molecular cloning and homology modelling of a subtilisin-like serine protease from the marine fungus, Engyodontium album BTMFS10.
An alkaline protease gene (Eap) was isolated for the first time from a marine fungus, Engyodontium album. Eap consists of an open reading frame of 1,161 bp encoding a prepropeptide consisting of 387 amino acids with a calculated molecular mass of 40.923 kDa. Homology comparison of the deduced amino acid sequence of Eap with other known proteins indicated that Eap encode an extracellular proteas...
متن کاملPurification and Characterization of Extracellular, Polyextremophilic α-amylase Obtained from Halophilic Engyodontium album
Background: a-Amylases (EC 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries. Objectives: The first ever detailed characterization of amylase from any halophilic Engyodontium album is presented. Materials and Methods: An extracellular α-amylase was studied from halophilic E. album TISTR 3645. The enzyme was e...
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This is the first reported case of native valve endocarditis caused by Engyodontium album. This fungus, rarely seen as a human pathogen, is separated from Tritirachium species by its lack of pigmentation and from Beauveria species by the presence of conidiogenous cells in whorls.
متن کاملpurification and characterization of extracellular, polyextremophilic α-amylase obtained from halophilic engyodontium album
background: a-amylases (ec 3.2.1.1) are covering approximately 25% of total enzyme market and are frequently used in food, pharmaceutical and detergent industries.objectives: the first ever detailed characterization of amylase from any halophilic engyodontium album is presented. materials and methods: an extracellular α-amylase was studied from halophilic e. album tistr 3645. the enzyme was ext...
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in the detergent industry. In this study, the extracellular alkaline serine protease gene, aprE, from Bacillusclausii was amplified by PCR and further cloned and expressed in B. subtilis WB600 using the pWB980 expression vector. Protease activity of the recombinant B. subtilis WB600 harboring the plasmid pWB980/aprEreached up to 1020 U/ml, approximately 3-folds higher than the nativ...
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ژورنال
عنوان ژورنال: Journal of Industrial Microbiology & Biotechnology
سال: 2010
ISSN: 1367-5435,1476-5535
DOI: 10.1007/s10295-010-0914-3