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Enzymatic activity of lipase in post-metamorphic phase bullfrogs Scientia Agricola
Braga,Luís Gustavo Tavares; Oliveira,Maria Goreti de Almeida; Lima,William Cardoso; Euclydes,Ricardo Frederico.
The knowledge of the digestive system of bullfrogs is an important step for the determination of their nutritional requirements throughout growth phases. With the objective of evaluating the enzymatic activity of lipase in the intestinal content of bullfrogs (Rana catesbeiana Shaw, 1802), 100 animals with median weight of 3.6 g were distributed in stalls under controlled temperature and photoperiod. The frogs, selected at the post-metamorphic phase, received commercial extruded diet ad libitum throughout the 87-day experiment. The collections of the intestinal content were performed by the desensitization of the frogs in ice and water at 0ºC and subsequent isolation of the small intestine. Determination of lipase activity was performed with a commercial...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Digestive enzyme; Frog culture; Specific activity.
Ano: 2006 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S0103-90162006000500004
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Improved purification process of β- and α-trypsin isoforms by ion-exchange chromatography BABT
Santos,Alexandre Martins Costa; Oliveira,Jamil Silvano de; Bittar,Eustáquio Resende; Silva,Anderson Lourenço da; Guia,Marcos Luiz dos Mares; Bemquerer,Marcelo Porto; Santoro,Marcelo Matos.
The purpose of this work was to improve the separation and yield of pure β- and α-trypsin isoforms by ion-exchange chromatography and to characterize some physical-chemical properties of these isoforms. Purification of trypsin isoforms was performed by ion-exchange chromatography in 0.1 mol/L tris-HC buffer, pH 7.10 at 4ºC. The sample loading, salt concentration, flow rate and pH of mobile phase were varied to determine their effects on the resolution of the separation. The resolution was optimized mainly between β- and α-trypsin. Pure isoforms were obtained by chromatographying 100 mg of commercial trypsin during seven days, yielding 51 mg of high purity β-trypsin and 13 mg of α-trypsin partially pure, with small amounts of contaminating of ψ-trypsin....
Tipo: Info:eu-repo/semantics/article Palavras-chave: Trypsin isoforms; Resolution; Ion-exchange chromatography; Purification; Specific activity; Mass spectrometry.
Ano: 2008 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1516-89132008000400009
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