Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp.

Extremophiles : Life Under Extreme Conditions
N SrideviAsmita A Prabhune

Abstract

A thermophilic microorganism producing bile salt hydrolase was isolated from hot water springs, Pali, Maharashtra, India. This microorganism was identified as Brevibacillus sp. by 16S rDNA sequencing. Bile salt hydrolase (BSH) was purified to homogeneity from this thermophilic source using Q-sepharose chromatography and its enzymatic properties were characterized. The subunit molecular mass of the purified enzyme was estimated to be 28 kDa by SDS-PAGE and, 28.2 kDa by MALDI-TOF analysis. The native molecular mass was estimated to be 56 kDa by gel filtration chromatography, indicating the protein to be a homodimer. The pH and temperature optimum for the enzyme catalysis were 9.0 and 60 degrees C, respectively. Even though BSH from Brevibacillus sp. hydrolyzed all of the six major human bile salts, the enzyme preferred glycine conjugated substrates with apparent K(M) and k(cat) values of 3.08 microM and 6.32 x 10(2) s(-1), respectively, for glycodeoxycholic acid. The NH(2)-terminal sequence of the purified enzyme was determined and it did not show any homology with other bacterial bile salt hydrolases. To our knowledge, this is the first report describing the purification of BSH to homogeneity from a thermophilic source.

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Citations

Aug 12, 2009·Applied Biochemistry and Biotechnology·Anil K PatelSudhir B Chincholkar
Nov 29, 2014·Critical Reviews in Biotechnology·Vellore Sunder AvinashCheravakkattu Gopalan Suresh
Oct 23, 2016·Biochimica Et Biophysica Acta. General Subjects·Deepak ChandSureshkumar Ramasamy
Jun 13, 2017·Molecular Aspects of Medicine·Sarah L LongSusan A Joyce
Aug 12, 2018·Protein Science : a Publication of the Protein Society·Zixing Dong, Byong H Lee
Feb 6, 2017·Animal Health Research Reviews·Wenjing Geng, Jun Lin
Sep 10, 2017·Archives of Microbiology·Abhijit Poddar, Subrata K Das

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