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Papamichael EM
Papamichael EM
Greece
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Research Article
Purification, Amino Acid sequencing and Thermostability of an Extracellular Low Molecular Weight Esterase Produced by Bacillus Subtilis NRRL 41270 in Fermentation
Author(s): Papagianni M and Papamichael EMPapagianni M and Papamichael EM
Extracellular esterase activity in Bacillus subtilis NRRL 41270 fermentation broths was found to reside in a small protein with a molecular weight less than 10 kDa. Following purification, esterase activity on fluorescein dibutyrate was estimated at 12 U/min/mg proteins. Enzyme saturation was observed at 5 μM substrate concentration. The produced esterase hydrolysed tributyrin. Its specific activity was estimated to be 17.8 μmol acid released/min/mg proteins. The small protein was subjected to size exclusion chromatography, SDS-PAGE and amino acid sequencing. Analysis revealed a sequence of the following amino acid residues: eevaetysfyhitphdystshispapvqffspap, according to which the molecule has 34 amino acid residues and a calculated molecular mass of 3853, which was in accordance with the gel filtration and SDS-PAGE results. Sequence based analysis and use of bioinformatics to.. View More»
DOI: 10.4172/1948-5948.1000353