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RLJ-NE-299A: A new plant based vaccine adjuvant
No full textAlum has been in use since long as an adjuvant for vaccines. However, its use as a vaccine adjuvant offers limitation in supporting cell mediated response. Therefore, a new plant based product RLJ-NE-299A from Picrorhiza kurroa reported for its immunostimulatory activity,
has been explored for its potential as an alternative adjuvant. In order to compare the adjuvant activity with alum, antigen-specific immune responses were evaluated following immunization with a formulation containing hepatitis B surface antigen (HBsAg) adjuvanted with RLJNE-
299A and alum in mice. The adjuvant RLJ-NE-299A up-regulated remarkably the expression of Th1 cytokines IL-2, IL-12, IFN-�,TNF � and Th2 cytokine IL-4 in lymph node cell cultures after 2 weeks of primary immunization with HBsAg. Further, the levels of both immunoglobulins IgG2a (Th1) and IgG1 (Th2) subtypes increased profoundly in blood sera of mice immunized with HBsAg/RLJ-NE-299A.
The results indicated that RLJ-NE-299A has strong potential to increase both cell mediated and humoral immune responses and is capable of sustaining the total antigen-specific antibody response. Besides, the RLJ-NE-299A provides a signal to gear up both CD4 helper cells (Th1 and Th2) and CD8 cells populations, which may have important implications for vaccination against hepatitis B virus. Variable doses of RLJ-NE-299A (0.312 1340 �g) containing vaccine antigen (HBsAg) were well tolerated with optimum T cell response at 2.5 �g/ml. Not only this, the adjuvant was also able to induce cellular immune responses to HBsAg as evidenced by Th1 and Th2 cytokines upregulation, which
enabled mice to overcome the unresponsiveness to antigen HBsAg encountered with alum-adjuvanted vaccine in otherwise non-responding mice population. The study presents evidence that the HPLC standardized fraction RLJ-NE-299A, is an adjuvant of choice over alum in improving and maintaining the improved immune status against HBsAg, and may also prove useful adjuvant candidate with other vaccine
antigens, too
A cold-active esterase of Streptomyces coelicolor A3(2): from genome sequence to enzyme activity
No full textThe genome sequence of Streptomyces coelicolor
A3(2) contains 51 putative lipase and esterase genes
mostly of unknown function. The gene estB (locus SCO
6966) was expressed as a His-tagged protein in E. coli.
Esterase B was active at low temperatures exerting its maximum activity at 30°C and retaining more than 25% of its
activity at 4°C. The optimum pH was 8–8.5. The enzyme
was active against short synthetic p-nitrophenylesters
(C2–C10) with maximum activity towards the acetate ester
(C2). The esterase was tested on 13 series of racemic esters
of potential interest for the synthesis of chiral pharmaceutical compounds. 4 of the series were substrates and a modestdegree of enantioselectivity was observed (enantiomeric ratios of 1.1–1.9)
Arthrobacter sp.: a lipase of choice for the kinetic resolution of racemic arylazetidinone precursors of taxanoid side chains
No full textThe native strain of Arthrobacter sp. (MTCC 5125) bearing a lipase has been found to be the most effective in the kinetic resolution of racemic arylazetidinones for producing cis-(3R,4S)-3-acetoxy-1-(4-methoxyphenyl)-4-phenyl-2-azetidinone, cis-(3R,4R)-3-acetoxy-1-(4-methoxyphenyl)-4-(2-furanyl)-2-azetidinone, cis-(3R,4R)-3-acetoxy 1-(4-methoxyphenyl)-4-(2-thienyl)-2-azetidinone, and cis-3-acetoxy-4-(t-butyl)-2-azetidinone products. The resolved compounds, which were obtained in high enantiopurity are important intermediates of amino acid side chains of paclitaxe
Chemically Standardized Isolates from Cedrus deodara Stem Wood having Anticancer Activity
No full textAn isolate ”CD lignan mixture” comprising lignans from stem wood of Cedrus deodara consisted of (-)-wikstromal (75 - 79 %), (-)-matairesinol (9 - 13 %) and benzylbutyrolactol (7 - 11 %) and was studied for its in vitro cytotoxcity against human cancer cell lines. The in vivo anticancer activity of CD lignan mixture was studied using Ehrlich ascites carcinoma and colon carcinoma (CA-51) models in mice. Its effect was also studied on annexin V binding, intracellular caspases and DNA fragmentation to gain insight into the mode of action. In vitro cytotoxicity studies showed significant dose-dependent effects against several cancer cell lines from different tissues such as breast, cervix, neuroblastoma, colon, liver, and prostrate at 10, 30 and 100 μg/mL. The IC50 values varied from 16.4 ng/mL to 116.03 μg/mL depending on the cell line. Comparative data of IC50 values of CD lignan mixture showed a synergistic effect in comparision to the individual molecules, i. e., (-)-matairesinol, (-)-wikstromol present in CD lignand mixture. CD lignan mixture had the most pronounced effect on CNS cell lines followed by colon. The tumor regression observed with Ehrlich ascites carcinoma and CA-51 was 53 % and ∼54 %, respectively, when CD lignan mixture was given at 300 mg/kg, i. p. for nine days in the Ehrlich ascites carcinoma model and 400 mg/kg, i. p. for the same period in the CA-51 model. It was comparable with 5-fluorouracil at 22 mg/kg and 20 mg/kg, respectively. CD lignan mixture at 10, 30 and 100 μg/mL increased the percentage of annexinV positive HL-60 cells to 1.9 - 17.18 % as compared to control (1.04 %). In K562 cells CD lignan mixture at 10, 30 or 100 μg/mL and staurosporine (1 μM) showed 9.13 %, 11.38 %, 17.22 % and 28.07 % intacellular caspases activation, respectively. A distinct DNA laddering pattern was observed for treatment with the CD lignan mixture in HL-60, K562 (30 μg/mL and 100 μg/mL) and MOLT-4 cells (30 μg/mL) after 24 h incubation. DNA cell cycle analysis indicated that CD lignan mixture at 10, 30 and 100 μg/mL increased the content of hypodiploid (sub G1 phase) cells when compared to control (2.55, 5.4 and 6.25 % vs. 0.27 %). The present study indicates that CD lignan mixture has cytotoxic potential against human cancer cell lines. It has the ability to induce tumor regression in vivo. It induces apoptosis as indicated by annexin V positive cells, induction of intracellular caspases, DNA fragmentation and DNA cell cycle analysis
Reaction of allenylmagnesium and allenylindium bromides with nitrile oxides: synthesis of novel 5-butynyl- and 5-methylisoxazoles
No full text5-Butynylisoxazoles were obtained in high yields through a domino addition, C–O heterocyclization involving allenylmagnesium bromide and benzonitrile oxide in dry THF, in which the corresponding 5-methylisoxazoles were isolated in trace amounts. However, when the reactions were attempted in aqueous media using allenylindium bromide, 5-methylisoxazoles were formed as the sole products in high yields
Addition of Allylindium Bromide to Nitrile Oxides in Aqueous Media: Convenient Synthesis of 5-Methylisoxazolines
No full text5-Methylisoxazolines were obtained in good yields through
a highly selective nucleophilic addition of allylindium reagent to benzonitrile oxides with concominant C–O heterocyclization
Lipase-catalyzed Separation of Geometrical Isomers: Geraniol 13Nerol
No full textThe substrate/lipase ratio as well as pH of the buffer medium played important roles in the resolution of geometrical isomeric mixture of geraniol 13nerol. Based on the results, an immobilized lipase from Pseudomonas fluorescens (PFL) was found effective in selective transesterifications whereas Pseudomonas sp. Lipase (PSL) was found to be useful in hydrolyzing the esters
A novel esterase from Bacillus subtilis (RRL 1789): Purification and characterization of the enzyme
No full textAn esterase (EC 3.1.1.1) produced by an isolated strain of Bacillus subtilis RRL 1789 exhibited moderate to high enantioselectivity in the kinetic resolution of several substrates like aryl carbinols, hydroxy esters, and halo esters. The enzyme named as B. subtilis esterase(BSE), was purified to >95% purity with a specific activity of 944 U/mg protein and 12% overall yield. The purified enzyme is �52 kDa monomer, maximally activity at 37 �C and pH 8.0 and fairly stable up to 55 �C. The enzyme does not exhibit the phenomenon of interfacial activation with tributyrin and p-nitrophenyl butyrate beyond the saturation concentration. The enzyme showed preference for triacyglycerols and esters of p-nitrophenol with short chain fatty acid. Presence of Ca2+ ions increases the activity of enzyme by �20% but its presence does not have any influence on the thermostability of the enzyme. The enzyme is not a metalloprotein and belongs to the
family of serine proteases. The N-terminal amino acid sequence of BSE determined, as Met-Thr-Pro-Glu-Iso-Val-Thr-Thr-Glu-Tyr-Glyrevealed similarity with the N-terminal amino acid sequence of p-nitrobenzylesterase of B. subtilis
Geranium (Pelargonium sp. ‘hybrid’) essential oil in subtropical and temperate regions of Jammu and Kashmir
No full textSix accessions of geranium (Pelargonium sp. ‘hybrid’) were introduced in temperate and subtropical regions of Jammu and Kashmir. The herbaceous parts in the commercial distillation gave 0.09–0.13% oil on fresh weight basis. The calculated herbage yield (tonnes/ha) and oil yield (litre/ha) varied from 31.5 ± 1.87 to 49.1 ± 2.73 and 32.40 to 57.12, respectively. The geranium oil produced in different regions of Jammu and Kashmir was comparable to that produced in other geranium-growing areas in India in terms of its major constituents, citronellol (22.5–34.5%) and geraniol (13.9–24.7%), respectively. This suggests that geranium can be successfully grown in the state of Jammu and
Kashmir. Copyright © 2006 John Wiley & Sons, Ltd
Arthrobacter sp. lipase immobilization for improvement in stability and enantioselectivity
No full textArthrobacter sp. lipase (ABL, MTCC no. 5125)is being recognized as an efficient enzyme for the
resolution of drugs and their intermediates. The immobilization of ABL on various matrices for its enantioselectivity,stability, and reusability has been studied. Immobilization by covalent bonding on sepharose and silica afforded a maximum of 380 and 40 IU/g activity, respectively,whereas sol 13gel entrapment provided a maximum of 150 IU/g activity in dry powder. The immobilized enzyme
displayed excellent stability in the pH range of 4 1310 and
even at higher temperature, i.e., 50 136