Master of Science in Biology (MS)
Ynalvez, Ruby A.
This study focused on the determination of the biological and biochemical properties of four purified commercial lectins from the Leguminosae. The anti-HIV reverse transcriptase activity of the lectins from Arachis hypogaea, Dolichos biflorus, Erythrina crista-galli, and Glycine max have not yet been reported. In addition, their antifungal, and antibacterial activities against Aspergillus niger, Candida albicans, Chaetomium globosum, Rhizopus stolonifer (+), Staphylococcus aureus, Klebsiella pneumoniae, Pseudomonas aeruginosa, and Enterococcus faecalis are not yet known. All of these microorganisms have developed resistance to treatments in the last few years. Consequently, this study characterizes and compares the lectin activities of A. hypogaea, D. biflorus, E. crista-galli, and G. max based on their antimicrobial, blood group specificity, thermal stability, and agglutination activities. Lectin activity was detected and compared via agglutination assays using bovine, horse, rabbit, and sheep erythrocytes. Arachis hypogaea lectin agglutinated bovine, horse, and rabbit erythrocytes. Dolichos biflorus lectin agglutinated sheep erythrocytes only. Erythrina cristagalli and Glycine max lectins agglutinated bovine, rabbit, and sheep erythrocytes. The stability of A. hypogaea, E. cristagalli, and G. max lectins was determined to be affected by temperature and pH. Temperature was determined to impact the ln specific activity at pH 5.2, pH 7.2, and pH 9.2. Time was determined to drastically impact the ln specific activity at 100°C, but not at 0°C and 50°C. The lectins were found to be devoid of antibacterial and antifungal activity against the microorganisms tested. The lectins in this study showed HIV reverse transcriptase inhibition activity. Glycine max lectin had the highest mean inhibition among the lectins tested in this study. The effects of G. max at different concentrations on percent inhibition was compared to Azidothymidine (AZT).
Gonzalez, Karla M., "The Determination of the Biological and Biochemical Properties of Four Purified Commercial Lectins from the Leguminosae" (2018). Theses and Dissertations. 78.