Bacteriostatic activity of con a lectin from Canavalia ensiformis

The aim of this work was to explore the therapeutic applications of Con A lectin from Canavalia ensiformis and to explore its antibacterial activity. Activity of lectin was quantified by their ability to agglutinate erythrocytes using Hemagglutination assay. Characterization and purity of Con A lectin was evaluated by using SDS-PAGE analysis. The reversal of hemagglutination activity of lectin was evaluated by using the sugars namely; mannose, galactose, lactose, fructose, glucose. The antibacterial activity of lectins was tested against Streptococcus mutans, Staphylococcus aureus, Bacillus subtilis, Escherichia coli using pour plate method. Amoxycillin was used as standard. At 250mg/ml concentration Con A lectin showed good bacteriostatic activity

Continuous hydrogenation of 2-butyne-1,4-diol to 2-butene- and butane-1,4-diols

Continuous catalytic hydrogenation of 2-butyne-1,4-diol (B<SUB>3</SUB>D) was carried out in a fixed-bed reactor over 1% Pt/CaCO<SUB>3 </SUB>catalyst to give 2-butene-1,4-diol (B<SUB>2</SUB>D) and butane-1,4-diol (B<SUB>1</SUB>D) without formation of any other side products. In case of continuous hydrogenation, higher selectivity (66%) to B<SUB>2</SUB>D could be obtained and the selectivity pattern was completely different from that found in case of batch slurry operation in which B<SUB>1</SUB>D selectivity was very much higher (83%) than the B<SUB>2</SUB>D selectivity (17%). Another interesting feature was that by varying the contact time, the selectivity to both B<SUB>2</SUB>D as well as B<SUB>1</SUB>D could be varied over a wide range which is an attractive option to obtain the desired products mix of B<SUB>1</SUB>D and B<SUB>2</SUB>D, depending on the fluctuation in the market demand. Further, a mathematical model for reactor performance was also developed on the basis of the kinetic data obtained previously in a batch slurry reactor. The predicted values of conversion, selectivity, and rate of hydrogenation were found to agree with the experimental data over a wide range of conditions

Comparison and Suitability of Gel Matrix for Entrapping Higher Content of Enzymes for Commercial Applications

To check the suitability of enzyme entrapped beads for use in pharmaceutical industry, amylase enzyme was entrapped in agar/agarose, polyacrylamide gels and calcium alginate beads. Sodium alginate of 1% concentration was found to be best with respect to immobilization efficiency and calcium alginate beads so obtained were not much susceptible to breakage. When sodium alginate- amylase mixture was added from a height of about 20-30 cm. into CaCl2 solution, size of beads was large at higher alginate concentration due to the increase in the size of droplet formation before entering into CaCl2 solution. Enzyme entrapped polyacrylamide and agar/agarose gels were fragile and could not withstand repeated use whereas enzyme entrapped in large calcium alginate beads was used successfully for 50 cycles for the conversion of starch into product without much damage to the beads under stirring conditions. Amylase preparation was also mixed with urease, lysozyme and coimmobilized in large sized calcium alginate beads. These beads were used for 10 repeated cycles to check the conversion of substrates into their products by their respective enzymes and we concluded that an enzyme or mixture of two or three enzymes can be immobilized in the same large sized calcium alginate beads. This will save the additional cost of bioreactor, manpower, maintenance conditions required for the conversion of one drug into another using enzyme/s entrapped in large sized beads