Copper II - polar amino acid complexes: toxicity to bacteria and larvae of Aedes aegypti

ABSTRACT Control strategies using insecticides are sometimes ineffective due to the resistance of the insect vectors.In this scenario new products must be proposed for the control of insect vectors.The complexes L-aspartate Cu (II) and L-glutamate-Cu (II) complexes were synthesized and characterized by elemental analysis, visible ultraviolet, infrared spectroscopy and potentiometric titration. The toxicity of these complexes was analyzed in Aedes aegypti (Diptera: Culicidae) larvae and Gram-negative and Gram-positive bacteria. The interaction between the ligands and the amino acid balance and the distribution of the species as a function of pH were discussed. The lethal concentration median (LC50) for Ae. aegypti larvae were: L-glutamic acid-Cu (II) - 53.401 mg L-1 and L-aspartate-Cu (II) - 108.647 mg L-1. The minimum inhibitory concentration (MIC) required for Staphylococcus aureus and Escherichia coli was: L-glutamate-Cu (II) 500-2000 mg L-1 and L-aspartate-Cu (II) 1000-2000 mg L-1. The concentrations demonstrated toxicity that evidence the potential of the complexes as bactericide and insecticide. Metal complexes formed by amino acids and transition metals are advantageous because of low environmental toxicity, biodegradability and low production cost.

Proximate composition and functional properties of Bulma cotton [Bombcapsis glabra] seeds

BOMBCAPSIS glabra seeds has percentage protein [16.50], crude fat [34.8], crude fibre [8.70] and ash [3.52] contents. The predominant mineral was potassium, 791mg/100g of sample. Palmitic acid was the predominant fatty acid constituting 75.0% in the seeds oil. The amino acid pattern of the seed flour showed that Aspartic and Glutamic acids were the major amino acids and that the seed flour was deficient in Leucine and Cystine. Physicochemical analysis of the seed oils showed that they could be classified as non-drying oils. Bombcarpsis glabra seed flour had high water and low oil absorption capacities 255.0 and 91.8%, respectively. It could serve as a good gelating agent with at least gelation concentration of 2.0%. The flour had poor foaming capacity but good foaming stability

Characterization and biological activities of Chenopodium leaf hemagglutinin (CLH).

A hemagglutinin (CLH) having native molecular mass of 58 kDa and subunit molecular mass of 33 kDa had been purified from the leaves of Chenopodium amaranticolor. The protein agglutinated rabbit erythrocytes and no agglutination was observed with any of the groups A, B or O of human blood. The amino acid composition revealed that CLH was rich in aspartic acid, glutamic acid, glycine and phenylalanine and also significant amount of methionine. The N-terminal amino acid sequence analysis showed that CLH had no homology with any of the plant hemagglutinins studied so far. It was inactive towards human peripheral blood cells but mitogenic for mouse spleen B-lymphocytes. CLH inhibited protein synthesis in rat thymocytes at high concentration. CLH did not inhibit TMV infection of leaves indicating absence of antiviral properties.