Levantamento malacológico da Bacia Hidrográfica do Lago Soledade, Ouro Branco, (Minas Gerais, Brasil) Malacological survey at the Soledade Lake, in Ouro Branco (Minas Gerais, Brazil)

Em estudo malacológico realizado na Bacia Hidrográfica do Lago Soledade, Ouro Branco, MG, no período de setembro de 1986 a março de 1991, foram coletados 46.579 moluscos, representados por 07 espécies de 05 famílias. Foram coletados 39.176 exemplares de Biomphalaria tenagophila, 1.296 de B. glabrata, sete exemplares de Drepanotrema cimex, 2.527 de Physa sp, 417 de Lymnaea sp, 92 de Pomacea haustrum e, a partir de março/1990, 3.064 exemplares de Melanoides tuberculata (Melanniidae = Thiaridae). Dos moluscos que apresentaram positividade para diversas larvas de trematódeos, quatro exemplares de B. tenagophila estavam positivos para S. mansoni.<br>A malacological survey was carried out at the Soledade Lake, in Ouro Branco, State of Minas Gerais, for the period 1986-1991. A total amount of 46,579 mollusks was collected, and among them seven species corresponding to five families could be found, as follows: 39,176 specimens of Biomphalaria tenagophila; 1,296 B. glabrata; 7 Drepanotrema cimex; 2,527 Physa sp; 417 Lymnaea sp; 92 Pomacea hastrum, and 3,064 specimens of Melanoides tuberculata (Melanniidae=Thiaridae) were collected from March/1990 onwards. Four specimens of B. tenagophila were found to be positive for Schistosoma mansoni

Liquid-liquid extraction of biomolecules in downstream processing - A review paper

Economic analysis shows that protein separation and purification are a very important aspect of biomolecules production and processing. This is particularly true for protein processing which, because of the complexity of the starting material, often requires many steps to reach the levels of purity required for medical and food applications. The separation specialists' task is to develop safe and simple processes to achieve products with a high level of purity. On a large scale, chromatography of proteins is not an easily applied method, although on a laboratory scale it is very effective and relatively simple. When it is scaled up, shortcomings such as discontinuity in the process, slow protein diffusion and large pressure drops in the system are seen. For these reasons a substantial research effort has been directed toward the use of aqueous two-phase systems (ATPSs) to replace the initial steps in protein purification and chromatography. This article reviews the chronology and main ATPS fundamentals and discuss the broader applications of this type of system in the extraction and separation of biomolecules