Purification and characterization of a novel extracellular esterase from pathogenic Streptomyces scabies that is inducible by zinc
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Biochemical Characterization of A Novel Thermophilic Esterase Isolated from Shewanella sp F88
The main objective of this study was to purify and characterize an esterase from Shewanella sp F88. The enzyme was purified 41-fold and an overall yield of 21 %, using a two-step procedure, including ammonium sulfate precipitation and Q-sepharore chromatography. Molecular weight of the enzyme was 62.3 kDa according to SDS-PAGE data. The enzyme showed an optimum activity at pH 6.5 and 58 ˚C. Evo...
متن کاملPurification and characterization of an acetyl xylan esterase produced by Streptomyces lividans.
The acetyl xylan esterase cloned homologously from Streptomyces lividans [Shareck, Biely, Morosoli and Kluepfel (1995) Gene 153, 105-109] was purified from culture filtrate of the overproducing strain S. lividans IAF43. The secreted enzyme had a molecular mass of 34 kDa and a pI of 9.0. Under the assay conditions with chemically acetylated birchwood xylan the kinetic constants of the enzyme wer...
متن کاملBiochemical and molecular characterization of the extracellular esterase from Streptomyces diastatochromogenes.
An esterase of Streptomyces diastatochromogenes was purified to homogeneity from culture filtrate. The purified enzyme had a molecular mass of 30,862 +/- 5.8 Da, as determined by electrospray mass spectrometry. The esterase-encoding gene was cloned on a 5.1-kb MboI fragment from S. diastatochromogenes genomic DNA into Streptomyces lividans TK23 by using plasmid vector pIJ702. Nucleotide sequenc...
متن کاملIdentification of a protein-binding sequence involved in expression of an esterase gene from Streptomyces scabies.
Expression of an esterase gene from Streptomyces scabies is regulated by zinc in both Streptomyces scabies and Streptomyces lividans. A specific protein-binding site was identified on an esterase promoter fragment by using an S-30 extract from S. scabies. The location of the protein-binding site was determined by gel shift assays of promoter deletion fragments and by DNase I footprinting analys...
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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ژورنال
عنوان ژورنال: Journal of Bacteriology
سال: 1987
ISSN: 0021-9193,1098-5530
DOI: 10.1128/jb.169.5.1967-1971.1987