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Pharmaceutical Purposes (pharmaceutical + purpose)
Selected AbstractsSupercritical fluid extraction of lipids from the heterotrophic microalga Crypthecodinium cohniiENGINEERING IN LIFE SCIENCES (ELECTRONIC), Issue 2 2010Ricardo Miguel Couto Abstract Microalgae biomass can be a feasible source of ,-3 fatty acids due to its stable and reliable composition. In the present study, the Crypthecodinium cohnii growth and docosahexaenoic acid (DHA, 22:6,3) production in a 100,L glucose-fed batch fermentation was evaluated. The lipid compounds were extracted by supercritical carbon dioxide (SC-CO2) from C. cohnii CCMP 316 biomas, was and their fatty acid composition was analysed. Supercritical fluid extraction runs were performed at temperatures of 313 and 323,K and pressures of 20.0, 25.0 and 30.0,MPa. The optimum extraction conditions were found to be 30.0,MPa and 323,K. Under those conditions, almost 50% of the total oil contained in the raw material was extracted after 3,h and the DHA composition attained 72%,w/w of total fatty acids. The high DHA percentage of total fatty acids obtained by SC-CO2 suggested that this extraction method may be suitable for the production of C. cohnii value added products directed towards pharmaceutical purposes. Furthermore, the fatty acid composition of the remaining lipid fraction from the residual biomass with lower content in polyunsaturated fatty acids could be adequate for further uses as feedstock for biodiesel, contributing to the economy of the overall process suggesting an integrated biorefinery approach. [source] COMPARATIVE STUDY OF MICROENCAPSULATION OF CASEIN HYDROLYSATES IN LIPOSPHERES AND LIPOSOMESJOURNAL OF FOOD BIOCHEMISTRY, Issue 1 2004HARRIMAN ALEY MORAIS The encapsulation in lipospheres and in liposomes was used with the aim of masking the bitterness of casein hydrolysates for dietetic of pharmaceutical purposes. Papain was used for preparing three casein hydrolysates, employing different temperatures and E:S ratios. The percentage of encapsulation of these preparations was measured by second derivative spectrophotometry (SDS). Lipid oxidation over a period of 60 days, was followed by quantifying the 2-thiobarbituric acid reactive substances (TBARS). Other analysis were performed for characterizing these vesicles, including the sensory evaluation and the measure of hydrophobicity. The results showed that these two encapsulation systems were equally efficient in reducing the hydrophobicity and the bitterness of casein hydrolysates. SDS was a useful tool in the characterization of these preparations. It is a quick and relatively low-cost method, and indicated that the encapsulation rate in lipospheres (65%) was higher than in liposomes (59%). The TBARS method revealed the chemical stability of these preparations over the period of study (60 days). [source] Papain hydrolysates of casein: molecular weight profile and encapsulation in lipospheresJOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, Issue 14 2004Cristiane MS Barbosa Abstract Some reaction parameters were tested in the hydrolysis of casein by papain, in order to prepare hydrolysates with high oligopeptide contents, for either dietetic or pharmaceutical purposes. Five casein hydrolysates were prepared and then fractionated by size-exclusion HPLC. The rapid correct fraction area method was used for quantifying peptides and free amino acids. Among the five reaction conditions tested, three produced similar peptide profiles. However, the use of a temperature of 37°C and an E:S ratio of 2% is probably the most economical condition for use in large-scale manufacture. With the aim of masking the bitterness of these preparations, a new method, based on the encapsulation in lipospheres, was used. Also, second derivative spectrophotometry was used for the first time to measure the extent of encapsulation of protein hydrolysates, which changed from 50% to 83%. Moreover, the efficiency of this system was evaluated by analysing other parameters, which showed a reduction of hydrophobicity and bitterness of all samples, as well as good chemical stability during 60 days of storage under refrigeration. The electron microscopical analysis of liposheres showed an average size around 5.0 ± 1.0 µm. Copyright © 2004 Society of Chemical Industry [source] Immobilized Metal Affinity Chromatography without Chelating Ligands: Purification of Soybean Trypsin Inhibitor on Zinc Alginate BeadsBIOTECHNOLOGY PROGRESS, Issue 1 2002Munishwar N. Gupta Immobilized metal affinity chromatography (IMAC) is a widely used technique for bioseparation of proteins in general and recombinant proteins with polyhistidine fusion tags in particular. An expensive and critical step in this process is coupling of a chelating ligand to the chromatographic matrix. This chelating ligand coordinates metal ions such as Cu2+, Zn2+, and Ni2+, which in turn bind proteins. The toxicity of chemicals required for coupling and their slow release during the separation process are of considerable concern. This is an important issue in the context of purification of proteins/enzymes which are used in food processing or pharmaceutical purposes. In this work, a simpler IMAC design is described which should lead to a paradigm shift in the application of IMAC in separation. It is shown that zinc alginate beads (formed by chelating alginate with Zn2+ directly) can be used for IMAC. As "proof of concept", soybean trypsin inhibitor was purified 18-fold from its crude extract with 90% recovery of biological activity. The dynamic binding capacity of the packed bed was 3919 U mL -1, as determined by frontal analysis. The media could be regenerated with 8 M urea and reused five times without any appreciable loss in its binding capacity. [source] | |||||||||||||