01734nas a2200241 4500008004100000020002200041022001400063245006700077210006600144260009900210300001400309490000800323520094300331100001801274700001601292700002101308700002001329700001001349700001201359700001201371700001101383856009801394 2007 eng d a978-0-444-53068-4 a0167-299100aImmobilization of Ntn hydrolases on APTES fuctionalized SBA-150 aImmobilization of Ntn hydrolases on APTES fuctionalized SBA15 aSara Burgerhartstraat 25, Po Box 211, 1000 AE Amsterdam, NetherlandsbElsevier Science BVcAUG a1891-18980 v1703 a

APTES Functionalized mesoporous silica SBA-15 molecular sieves have been prepared and used for immobilization of Penicillin G acylase. Physico chemical characterization was done by nitrogen adsorption, powder XRD and TEM methods to understand the nature of immobilized PGA enzyme. XRD data indicate a good mesoscopic order. The characteristic hexagonal features of SBA-15 were maintained in PGA immobilized SBA-15 samples. Incorporation of PGA does not affect the original pore structure of the parent SBA-15. The adsorption of PGA on SBA-15 from buffered solutions with a pH value, 7.8 has been studied as a model protein adsorption system. The maximum activity of the immobilized enzyme was observed at pH 7.8, slightly below the isoelectric point of the enzyme. The loading capacity of immobilized PGA is 34 mg protein per 0.5 g of SBA-15. The stability of Penicillin G acylase was enhanced by the physical entrapment in SBA-15.

1 aShah, Pallavi1 aSridevi, N.1 aPrabhune, Asmita1 aRamaswamy, Veda1 aXu, R1 aGao, Z.1 aChen, J1 aYan, W uhttps://library.ncl.res.in/content/immobilization-ntn-hydrolases-aptes-fuctionalized-sba-15-001413nas a2200253 4500008004100000022001400041245015500055210006900210260010200279300001200381490000800393520040600401653002900807653002600836653002500862653001700887100002000904700001400924700002100938700001900959700002100978700003000999856013001029 2008 eng d a0974-362600aIn situ synthesis of ligand reduced/capped silver nanoparticles and the effect of temperature and ligand structure on the size of silver nanoparticles0 aIn situ synthesis of ligand reducedcapped silver nanoparticles a aC V RAMAN AVENUE, SADASHIVANAGAR, P B \#8005, BANGALORE 560 080, INDIAbINDIAN ACAD SCIENCEScJAN a515-5200 v1203 a

We report in situ synthesis of silver nanoparticles using biosurfactants called sophorolipids as reducing and capping agents. We further study the effect of temperature and the structure of sophorolipid on the size of silver nanoparticles obtained. The silver nanoparticles were characterized by UV-visible, transmission electron microscope (TEM) and light scattering (DLS) analysis techniques.

10adynamic light scattering10aNucleation and growth10asilver nanoparticles10aSophorolipid1 aKasture, M., B.1 aPatel, P.1 aPrabhune, Asmita1 aRamana, C., V.1 aKulkarni, A., A.1 aPrasad, Bhagavatula L. V. uhttps://library.ncl.res.in/content/situ-synthesis-ligand-reducedcapped-silver-nanoparticles-and-effect-temperature-and-ligand02322nas a2200205 4500008004100000022001400041245014500055210006900200260007100269300001400340490000800354520149600362100002301858700002701881700002701908700002101935700002001956700001901976856012101995 2009 eng d a1932-744700aIn situ observation of antibiotic mediated concurrent growth of two distinct homogeneous populations of gold nanoparticles in solution phase0 aIn situ observation of antibiotic mediated concurrent growth of  a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcMAR a3478-34860 v1133 a

We report the observation of the unusual nucleation and growth kinetics of gold nanoparticles synthesized in the presence of the antibiotic cephalexin using in situ static and dynamic light scattering in conjunction with in situ UV-vis absorption measurements and transmission electron microscopy. Following a brief latency period, two well-separated populations of gold nanoparticles, with average sizes of 1-2 nm versus several tens of nanometer, respectively, nucleate simultaneously. For either size regime, the total number of particles increased rapidly, while their mean size and relative frequency remained essentially constant over a growth period of 5 h. With increasing temperature, the morphology of the larger nanoparticles became increasingly spherical, as indicated by the noticeable blue shift of the plasmon frequency for these particles. The detailed morphology for either particle population was confirmed with TEM. To our knowledge, this is the first observation of simultaneous growth of two distinct populations of crystalline nanoparticles in the solution phase. The coupled growth of two distinct populations of nuclei, their tight control of size but rapid increase in overall numbers present novel and intriguing facets of this antibiotic-mediated solution-growth of gold nanoparticles. The size evolution of the Mie-frequency exhibits a noticeable blue shift as the temperature increases, correlating with the roundness of the particle/bimodal distribution.

1 aJagannathan, Ramya1 aParmar, Avanish, Singh1 aAdyanthaya, Suguna, D.1 aPrabhune, Asmita1 aMuschol, Martin1 aPoddar, Pankaj uhttps://library.ncl.res.in/content/situ-observation-antibiotic-mediated-concurrent-growth-two-distinct-homogeneous-001733nas a2200277 4500008004100000022001400041245011000055210006900165260007900234300001200313490000800325520075200333653002201085653001701107653001501124653001101139653002401150653001301174100002501187700002201212700002701234700002401261700002401285700002101309856012501330 2011 eng d a0273-228900aIsolation, identification and optimization of a new extracellular lipase producing strain of rhizopus sp.0 aIsolation identification and optimization of a new extracellular a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcAUG a969-9780 v1643 a

A lipolytic mesophilic fungus which produces lipase extracellularly was isolated from soil. Based on ITS1-5.8S-ITS4 region sequences of ribosomal RNA, it was concluded that the isolate JK-1 belongs to genus Rhizopus and clades with Rhizopus oryzae. The present paper reports the screening, isolation, identification, and optimization of fermentation conditions for the production of lipase (EC 3.1.1.3). Culture conditions were optimized, and the highest lipase production was observed in basal medium with corn steep liquor as nitrogen source and glucose as carbon source. Maximum lipase production was observed at 72 h, which is about 870 U/ml. Optimization of fermentation conditions resulted in 16-fold enhancement in enzyme production.

10aCorn steep liquor10aFermentation10aITS region10aLipase10aMedium optimization10aRhizopus1 aKantak, Jayshree, B.1 aBagade, Aditi, V.1 aMahajan, Siddharth, A.1 aPawar, Shrikant, P.1 aShouche, Yogesh, S.1 aPrabhune, Asmita uhttps://library.ncl.res.in/content/isolation-identification-and-optimization-new-extracellular-lipase-producing-strain-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

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.

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-002008nas a2200169 4500008004100000245009300041210006900134260000800203300001400211490000800225520140700233100002001640700001801660700002101678700001701699856012201716 2016 eng d00aInhibition of quorum-sensing-mediated biofilm formation in Cronobacter sakazakii strains0 aInhibition of quorumsensingmediated biofilm formation in Cronoba cSEP a1708-17140 v1623 aThe present study investigated plant extracts for their anti-quorum-sensing (QS) potential to inhibit the biofilm formation in Cronobacter sakazakii strains. The bioassay based on loss of pigment production by Chromobacterium violaceum 026 and Agrobacterium tumefaciens NTL4 (pZLR4) was used for initial screening of the extracts. Further, the effect of extracts on the inhibition of QS-mediated biofilm in C. sakazakii isolates was evaluated using standard crystal violet assay. The effect on biofilm texture was studied using SYTO9 staining and light and scanning electron microscopy. Among the tested extracts, Piper nigrum and Cinnamomum verum at 100 ppm resulted in 78 and 68% reduction in the production of violacein as well as blue-green colour in both biosensor strains. A higher inhibitory activity (>50 %) on biofilm formation in C. sakazakii was observed for Pip. nigrum and Cin. verum, whereas the other extracts possessed moderate (25-50 %) and minimal (<25 %) inhibitory activities. Further, the fluorescent and scanning electron microscopic images indicated a major disruption in the architecture of biofilms of tested strains by Pip. nigrum. This study points to the possibility of using Pip. nigrum and Cin. verum as inhibitor of QS-mediated biofilm formation by C. sakazakii that could be further explored for novel bioactive molecules to limit the emerging infections of C. sakazakii1 aSingh, Niharika1 aPatil, Amrita1 aPrabhune, Asmita1 aGoel, Gunjan uhttps://library.ncl.res.in/content/inhibition-quorum-sensing-mediated-biofilm-formation-cronobacter-sakazakii-strains