@article { ISI:000266071900010, title = {Brevibacillus sp: a novel thermophilic source for the production of bile salt hydrolase}, journal = {Applied Biochemistry and Biotechnology}, volume = {157}, number = {2}, year = {2009}, month = {MAY}, pages = {254-262}, publisher = {HUMANA PRESS INC}, address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA}, abstract = {

A thermophilic microorganism growing within the temperature range of 40-65 A degrees C (optimum at 55 A degrees C) was isolated from hot water springs near Konkan, Maharashtra, India. Based on 16S rDNA sequence analysis, it was concluded that the isolate belongs to the genus Brevibacillus. The present paper reports the isolation, identification, and standardization of fermentation conditions for the production of enzyme, bile salt hydrolase (EC 3.5.1.24) which is produced intracellularly at high temperatures. This is the first report regarding the production of bile salt hydrolase from a thermophilic source. Optimization of fermentation conditions resulted in a 2.9-fold enhancement in enzyme production.

}, keywords = {Bile salt hydrolase, Brevibacillus sp, Fermentation, Glycodeoxycholic acid, Hot springs, Thermophile}, issn = {0273-2289}, doi = {10.1007/s12010-008-8326-9}, author = {Sridevi, N. and Prabhune, Asmita} } @article { ISI:000263784200014, title = {Characterization of the smallest dimeric bile salt hydrolase from a thermophile brevibacillus sp.}, journal = {Extremophiles}, volume = {13}, number = {2}, year = {2009}, month = {MAR}, pages = {363-370}, publisher = {SPRINGER JAPAN KK}, address = {CHIYODA FIRST BLDG EAST, 3-8-1 NISHI-KANDA, CHIYODA-KU, TOKYO, 101-0065, JAPAN}, 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 60A 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 mu M and 6.32 x 10(2) s(-1), respectively, for glycodeoxycholic acid. The NH2-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.

}, keywords = {Bile salt hydrolase, Brevibacillus sp., Dimeric intracellular enzyme, Purification, Thermophile}, issn = {1431-0651}, doi = {10.1007/s00792-008-0224-0}, author = {Sridevi, N. and Srivastava, Sameer and Khan, Bashir Mohammad and Prabhune, Asmita Ashutosh} } @article { ISI:000266197300018, title = {Hypocholesteremic effect of bile salt hydrolase from Lactobacillus buchneri ATCC 4005}, journal = {Food Research International}, volume = {42}, number = {4}, year = {2009}, note = {International Congress on Bioprocesses in Food Industries, Hyderabad, INDIA, NOV 06-08, 2008}, month = {MAY}, pages = {516-520}, publisher = {ICBF Forum; Biotech Res Soc India}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

The effect of oral administration of the immobilized bile salt hydrolase enzyme on serum cholesterol. triglyceride, high density lipoprotein levels and its application in the therapeutic treatment of hypercholesteremia was assessed. Culture conditions were optimized for the production of bile salt hydrolase, which resulted in 2.9-fold enhancement in activity. Bile salt hydrolase (BSH; E.C.3.5.1.24) was isolated from Lactobacillus buchneri ATCC 4005 and immobilized in 0.5\% gellan gum gel. The immobilized enzyme was orally delivered in wistar rats, induced with hypercholesteremia by triton X-100. The serum cholesterol and triglycerides were reduced by 50\% and 15\%, respectively, in the group fed with immobilized enzyme 10 IU/kg dose whereas administration of 20 IU/kg immobilized enzyme resulted in reduction of serum cholesterol by 58\% and triglycerides by 45\%, respectively. The results indicate that bile salt hydrolase has potential cholesterol lowering property and oral administration of the immobilized enzyme is an alternative pharmacological approach to reduce serum cholesterol levels. (C) 2009 Elsevier Ltd. All rights reserved.

}, keywords = {Bile salt hydrolase, Gellan gum, Hypocholesteremic effect, Lactobacillus buchneri, Wistar Rats}, issn = {0963-9969}, doi = {10.1016/j.foodres.2009.02.016}, author = {Sridevi, N. and Vishwe, Pradnya and Prabhune, Asmita} } @article { ISI:000330603800033, title = {Immobilization of bile salt hydrolase enzyme on mesoporous SBA-15 for co-precipitation of cholesterol}, journal = {International Journal of Biological Macromolecules}, volume = {63}, year = {2014}, month = {FEB}, pages = {218-224}, publisher = {ELSEVIER SCIENCE BV}, address = {PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS}, abstract = {

We describe herein a simple and effective strategy for immobilization of bile salt hydrolase enzyme by grafting glutaraldehyde groups inside channels of APTES functionalized SBA-15. The increase in glutaraldehyde concentration prevents leakage of enzyme but showed a steep decrease in enzyme activity in the immobilized matrix. So the degree of cross-linking should be the minimum possible to ensure sufficient stability without loss of activity. Cross-linking carried out with 0.1\% glutaraldehyde concentration showed the highest activity, so this was used in all further experiments. Physico-chemical characterizations of the immobilized enzyme were carried out by XRD, N-2 adsorption, TEM, FUR and Si-29 CP-MAS NMR techniques. Immobilized BSH exhibits enhanced stability over a wide pH (3-11) and temperature range (40-80 degrees C) and retains an activity even after recycling experiments and six months of storage. From our in vivo research experiment toward co-precipitation of cholesterol, we have shown that immobilized BSH enzyme may be the promising catalyst for the reduction of serum cholesterol levels in our preliminary investigation. Enhancement in pH stability at the extreme side of pH may favor the use of immobilized BSH enzyme for drug delivery purpose to with stand extreme pH conditions in the gastrointestinal conditions. (C) 2013 Elsevier B.V. All rights reserved.

}, keywords = {Bile salt hydrolase, Co-precipitation of cholesterol, SBA-15}, issn = {0141-8130}, doi = {10.1016/j.ijbiomac.2013.11.008}, author = {Bhange, Pallavi and Sridevi, N. and Bhange, Deu S. and Prabhune, Asmita and Ramaswamy, Veda} }