PurificaÃÃo e caracterizaÃÃo de proteases do Saramunete, Pseudupeneus maculatus, (Teleostei â Mullidae), Bloch, 1793

AUTOR(ES)
DATA DE PUBLICAÇÃO

2004

RESUMO

Trypsin-like enzyme was partially purified from the intestine and pyloric caeca of spotted goatfish (Pseudupeneus maculatus) by a simple four steps procedure (heat treatment, ammonium sulfate precipitation, Ammonium sulfate dialysis and Sephadex G-75 filtration). The enzymes from the intestine and pyloric caeca were 96-fold and 57.7-fold purified, respectively, according to this procedure, and yields of 68.1% and 26.1% were achieved, respectively. The proteins collected from the Sephadex G-75 filtration showed one single band in SDS-PAGE, molecular weight of 24.5 kDa and were able to hydrolyze casein. Both enzymes presented identical optima pH (9.0) and temperature (55oC). They lost half of this activity when incubated at this temperature for 30 min. Km for the trypsin-like enzyme from the intestine and pyloric caeca were 3.23 Â 0.04 mM (n =7) and 1.86 Â 0.26 mM (n = 8),respectively. This statistically difference in Km was the unique discrepancy between these enzymes. Finally, their activities were inhibited by the following ions in decreasing order: Al3+>Zn2+>Hg2+=Cu2+>Cd2+. The effects of Ca2+, Mg2+, Mn2+, Ba2+, K+1, Li+1 and Co2+ were statistically significant

ASSUNTO(S)

enzima trypsin pseudupeneus maculatus protease spotted goatfish pseudupeneus maculatus protease tripsina tropical fish enzyme bioquimica saramunete peixe tropical

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