01541nas a2200229   4500008004100000022001400041245009200055210006900147260007900216300001200295490000800307520072400315653002401039653002101063653001701084653002601101653001601127653001601143100001601159700002101175856011501196       2009                        eng d  a0273-228900aBrevibacillus sp: a novel thermophilic source for the production of bile salt hydrolase0 aBrevibacillus sp a novel thermophilic source for the production   a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcMAY  a254-2620 v1573 a<p>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.</p>10aBile salt hydrolase10aBrevibacillus sp10aFermentation10aGlycodeoxycholic acid10aHot springs10aThermophile1 aSridevi, N.1 aPrabhune, Asmita  uhttps://library.ncl.res.in/content/brevibacillus-sp-novel-thermophilic-source-production-bile-salt-hydrolase-001995nas a2200229   4500008004100000022001400041245009000055210006900145260008700214300001200301490000700313520115800320653002401478653001501502653002901517653002701546653001601573100001601589700002001605700002101625856011901646       2009                        eng d  a0963-996900aHypocholesteremic effect of bile salt hydrolase from Lactobacillus buchneri ATCC 40050 aHypocholesteremic effect of bile salt hydrolase from Lactobacill  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbICBF Forum; Biotech Res Soc IndiacMAY  a516-5200 v423 a<p>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.</p>10aBile salt hydrolase10aGellan gum10aHypocholesteremic effect10aLactobacillus buchneri10aWistar Rats1 aSridevi, N.1 aVishwe, Pradnya1 aPrabhune, Asmita  uhttps://library.ncl.res.in/content/hypocholesteremic-effect-bile-salt-hydrolase-lactobacillus-buchneri-atcc-4005-002250nas a2200229   4500008004100000022001400041245010600055210006900161260007300230300001200303490000700315520140000322653002401722653003601746653001101782100002001793700001601813700002001829700002101849700002001870856013001890       2014                        eng d  a0141-813000aImmobilization of bile salt hydrolase enzyme on mesoporous SBA-15 for co-precipitation of cholesterol0 aImmobilization of bile salt hydrolase enzyme on mesoporous SBA15  aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcFEB  a218-2240 v633 a<p>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.</p>10aBile salt hydrolase10aCo-precipitation of cholesterol10aSBA-151 aBhange, Pallavi1 aSridevi, N.1 aBhange, Deu, S.1 aPrabhune, Asmita1 aRamaswamy, Veda  uhttps://library.ncl.res.in/content/immobilization-bile-salt-hydrolase-enzyme-mesoporous-sba-15-co-precipitation-cholesterol-001909nas a2200217   4500008004100000022001400041245016500055210006900220260007900289300001200368490000800380520103200388653001601420653002401436653001001460653002101470653003101491100002201522700002101544856012601565       2015                        eng d  a0273-228900aPossible correlation between bile salt hydrolysis and ahl deamidation: staphylococcus epidermidis RM1, a potent quorum quencher and bile salt hydrolase producer0 aPossible correlation between bile salt hydrolysis and ahl deamid  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcMAY  a140-1500 v1763 a<p>The aim of the present work was to isolate a bile salt hydrolase (BSH) producer from fermented soy curd and explore the ability of the BSH produced to cleave bacterial quorum sensing signals. Bacterial isolates with possible ability to deconjugate bile salts were enriched and isolated on De Man, Rogosa and Sharpe (MRS) medium containing 0.2 % bile salts. BSH-producing positive isolate with orange-pink-pigmented colonies was isolated and was identified as a strain of Staphylococcus epidermidis using biochemical and phylogenetic tools. S. epidermidis RM1 was shown to possess both potent BSH and N-acyl homoserine lactone (AHL) cleavage activity. Genetic basis of this dual-enzyme activity was explored by means of specific primers designed using S. epidermidis ATCC 12228 genome as template. It was observed that a single enzyme was not responsible for both the activity. Two different genetic elements corresponding to each of the enzymatic activity were successfully amplified from the genomic DNA of the isolate.</p>10aAHL acylase10aBile salt hydrolase10aCV02610aQuorum quenching10aStaphylococcus epidermidis1 aMukherji, Ruchira1 aPrabhune, Asmita  uhttps://library.ncl.res.in/content/possible-correlation-between-bile-salt-hydrolysis-and-ahl-deamidation-staphylococcus-0