Brazilian Archives of Biology and Technology (Mar 2001)

Purification and characterisation of trypsin-like enzyme from the pyloric caeca of cod (Gadus morhua) II

  • Luiz Henrique Beirão,
  • Ian Mckintoch Mackie,
  • Evanilda Teixeira,
  • César Damian

DOI
https://doi.org/10.1590/S1516-89132001000100005
Journal volume & issue
Vol. 44, no. 1
pp. 33 – 40

Abstract

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A trypsin -like enzyme from the pyloric caeca of cod (Gadus morhua) was purified by affinity chromatography on CHOM Sepharose 4B. Some characteristics were established by its catalytic activity on T.A.M.E., typical enzyme substrate, and serine protease inhibitors. The enzyme had an isoelectric point of 5.30 and 5.89 and was very similar in amino acid composition to bovine trypsin, but differed in having a higher relative amount of acidic amino acids and a lower amount of basic amino acids. The enzyme also hydrolysed fish protein substrates.A tripsina do ceco pilórico do bacalhau (Gadus morhua) foi purificada por cromatografia de CHOM Sepharose 4B. Algumas características foram determinadas como atividade catalítica para T.A.M.E., substratos enzimáticos e inibidores de proteases. A enzima mostrou ponto isoelétrico de 5,30 e 5,89 e composição de aminoácidos similar à tripsina bovina, mas diferiu por ter um alto percentual de aminoácidos ácidos e baixo valor em aminoácidos básicos. A tripsina do bacalhau também hidrolisou substratos de proteínas de pescados.

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