Corrigendum: Characterization of ML-005, a Novel Metaproteomics-Derived Esterase
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چکیده
منابع مشابه
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...
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[This corrects the article on p. 1460 in vol. 8, PMID: 28824588.].
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The product YkoN of the gene of unknown function, ykoN, of Bacillus subtilis Marburg has the pentapeptide lipase/esterase motif (Gly-X-Ser-X-Gly), and thus YkoN is expected to have a lipase or esterase activity. To characterize the expected enzyme activity the plasmid having a modified ykoN that include the sequence for His(x6) tag at its C-terminus of YkoN, which has 373 amino acid residues, w...
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متن کاملbiochemical 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...
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ژورنال
عنوان ژورنال: Frontiers in Microbiology
سال: 2018
ISSN: 1664-302X
DOI: 10.3389/fmicb.2018.02716