Fracionamento do veneno da Apis mellifera utilizando membranas de ultrafiltração de celulose regenerada de 10 KDA

• Ano de defesa: 2015
• Autor(a) principal: Júlio César Moreira de Brito
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Minas Gerais; UFMG
• Palavras-chave em Português: Ultrafiltração; Apitoxina; Melitina; Membrana; Fosfolipase A2; Engenharia quimica
• Link de acesso: http://hdl.handle.net/1843/BUBD-A3CGCY

The venom from Apis mellifera is a mixture of several peptides and carbohydrates whose main compounds are melittin, phospholipase A2, apamin, secapin, tertiapin, adolapin, MCD peptide, hyaluronidase and fosfomonoesterases. Some of these components have pharmacological applications and their use in therapy has been increasing in recent years. At the same time, some of these components have allergenicity, and their presence can result in compounds with high allergenic potential. Melittin and phospholipase A2 are the most numerous peptides present in Apis mellifera venom and together may constitute approximately 70% of its dry weight. Phospholipase A2 e (19 kDa), hyaluronidase (38 kDa) and phosphomonoesterase (38 kDa) are the most allergenic substances present and each has a molecular mass greater than the great majority of peptides present in the venom, such as melittin (2.84 kDa). A reduction of the prevalence of these allergenic compounds was obtained using ultrafiltration with 10 kDa membranes of regenerated cellulose. These membranes showed a hydraulic permeability value 30% below the levels defined by the membrane manufacturer. The values obtained in N2 physisorption corroborated the results of the images obtained using scanning electron microscopy. Established process parameters tested limited flows to bee venom of 115, 85 and 50 kg/m2.h for concentrations of 10, 30 and 50 g/L respectively. The apitoxin concentration of 1 g/L was measured and showed a better permeability for melittin, approximately 60%, and a better retention of phospholipase A2, at approximately 60%. The phospholipase A2 present in the permeate showed no activity, evidence of a possible denaturation of this enzyme due to its passage through the membrane pores. This experiment showed ultrafiltration to be an effective technique for the reduction of major apitoxin allergens.