Enrichment of Eicosapentaenoic Acid from Sardine Oil with Δ5-Olefinic Bond Specific Lipase from Bacillus licheniformis MTCC 6824

2008 ◽  
Vol 56 (4) ◽  
pp. 1428-1433 ◽  
Author(s):  
Kajal Chakraborty ◽  
R. Paulraj
Keyword(s):  
Eicosapentaenoic Acid ◽  
Bacillus Licheniformis ◽  
Olefinic Bond ◽  
Sardine Oil

Preparation of eicosapentaenoic acid concentrates from sardine oil by Bacillus circulans lipase

2010 ◽  
Vol 120 (2) ◽  
pp. 433-442 ◽  
Author(s):  
Kajal Chakraborty ◽  
P. Vijayagopal ◽  
Rekha D. Chakraborty ◽  
K.K. Vijayan
Keyword(s):  
Eicosapentaenoic Acid ◽  
Bacillus Circulans ◽  
Sardine Oil

scholarly journals Sardine Fish Oil By Sentrifugation and Adsorbent for Emulsion

2017 ◽  
Vol 20 (1) ◽  
pp. 84 ◽  
Author(s):  
Kristina Haryati ◽  
Sugeng Heri Suseno ◽  
Nurjanah Nurjanah
Keyword(s):  
Citric Acid ◽  
Eicosapentaenoic Acid ◽  
Fish Oil ◽  
Carboxymethyl Cellulose ◽  
Fruit Juice ◽  
Fish Meal ◽  
Secondary Oxidation ◽  
Oil Emulsion ◽  
Sardine Oil ◽  
Oxidation Parameters

Sardine fish meal by-product contain eicosapentaenoic acid (EPA) and docosahexaenoic (DHA) and it can be made as emulsion. The purpose of this study were to determine the best fish oil emulsion by mixing<br />the oil phase (lecithin 3% and oil) and water phase (carboxymethyl cellulose/CMC 2% and fruit juice) and then stored until creaming, and the emulsion is analyzed their viscosity, pH, percent of stability and long<br />separation. Sardine oil is separated from the emulsion and tested oxidation parameters. The best emulsion was fish oil emulsion after refined without citric acid (RTS) with viscosity (2470.31 cP), pH (5.64), percent of stability (56.14%) and long separation (14 days). Primary and secondary oxidation parameters of RTS  were FFA (14.87%), PV (14.43 meq/kg), AV (32.57 meq KOH/g), AnV (17.3 meq/kg), and Totox (46.16 meq/kg).

Microanatomy of the Periplasm of Bacillus Licheniformis

1971 ◽  
Vol 29 ◽  
pp. 262-263
Author(s):  
B.K. Ghosh
Keyword(s):  
Cell Wall ◽  
Plasma Membrane ◽  
Bacillus Licheniformis ◽  
External Environment ◽  
Permeability Barrier ◽  
Periplasmic Space ◽  
Modified Technique ◽  
Gram Positive ◽  
Gram Negative ◽  
Gram Positive Bacteria

Periplasm of bacteria is the space outside the permeability barrier of plasma membrane but enclosed by the cell wall. The contents of this special milieu exterior could be regulated by the plasma membrane from the internal, and by the cell wall from the external environment of the cell. Unlike the gram-negative organism, the presence of this space in gram-positive bacteria is still controversial because it cannot be clearly demonstrated. We have shown the importance of some periplasmic bodies in the secretion of penicillinase from Bacillus licheniformis.In negatively stained specimens prepared by a modified technique (Figs. 1 and 2), periplasmic space (PS) contained two kinds of structures: (i) fibrils (F, 100 Å) running perpendicular to the cell wall from the protoplast and (ii) an array of vesicles of various sizes (V), which seem to have evaginated from the protoplast.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

Eicosapentaenoic Acid Interferes with U46619-Stimulated Formation of Inositol Phosphates in Washed Rabbit Platelets

1989 ◽  
Vol 62 (04) ◽  
pp. 1116-1120 ◽  
Author(s):  
N Chetty ◽  
J D Vickers ◽  
R L Kinlough-Rathbone ◽  
M A Packham ◽  
J F Mustard
Keyword(s):  
Signal Transduction ◽  
Fatty Acid Composition ◽  
Eicosapentaenoic Acid ◽  
Inositol Phosphates ◽  
Inositol Phosphate ◽  
Dense Granule ◽  
Detectable Change ◽  
Membrane Phospholipids ◽  
Rabbit Platelets ◽  
Stimulation Of

SummaryEicosapentaenoic acid (EPA) inhibits platelet responsiveness to aggregating agents. To investigate the reactions that are affected by EPA, we examined the effect of preincubating aspirintreated rabbit platelets with EPA on stimulation of inositol phosphate formation in response to the TXA2 analogue U46619. Stimulation of platelets with U46619 (0.5 μM) caused aggregation and slight release of dense granule contents; aggregation and release were inhibited by preincubation of the platelets with EPA (50 μM) for 1 h followed by washing to remove unincorporated EPA. Incubation with EPA (50 μM) for 1 h did not cause a detectable increase in the amount of EPA in the platelet phospholipids. When platelets were prelabelled with [3H]inositol stimulation with U46619 of control platelets that had not been incubated with EPA significantly increased the labelling of mos1tol phosphates. The increases in inositol phosphate labelling due to U46619 at 10 and 60 s were partially inhibited by premcubat10n of the platelets with 50 μM EPA. Since the activity of cyclo-oxygenase was blocked with aspirin, inhibition of inositol phosphate labelling in response to U46619 indicates either that there may be inhibition of signal transduction without a detectable change in the amount of EPA in platelet phospholipids, that changes in signal transduction require only minute changes in the fatty acid composition of membrane phospholipids, or that after a 1 h incubation with EPA, activation of phospholipase C is affected by a mechanism that is not directly related to incorporation of EPA.

Decrease of Platelet Activity After Intake of Small Amounts of Eicosapentaenoic Acid in Diabetics

1982 ◽  
Vol 48 (03) ◽  
pp. 344-344 ◽  
Author(s):  
B Velardo ◽  
M Lagarde ◽  
M Guichardant ◽  
M Dechavanne ◽  
M Beylot ◽  
...  
Keyword(s):  
Eicosapentaenoic Acid ◽  
Platelet Activity

Dunaliella salina Teod. as a Prominent Source of Eicosapentaenoic Acid

2010 ◽  
Vol 12 (2) ◽  
pp. 185-189 ◽  
Author(s):  
Rahul A. Bhosale ◽  
M. P. Rajabhoj ◽  
B. B. Chaugule
Keyword(s):  
Eicosapentaenoic Acid ◽  
Dunaliella Salina
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