Properties of Trypsin from the Pyloric Ceca of Atlantic Cod (Gadus morhua)
ABSTRACT Trypsin (EC 3.4.21.4) was isolated from the pyloric ceca of Atlantic cod and purified to homogeneity by affinity chromatography. The enzyme catalyzed the hydrolysis of benzoyl arginine p ‐nitroanilide (BAPA, pH 8.2 and 25°C) such that V max was 250 BAPA units per micromole trypsin and K m w...
| Published in: | Journal of Food Science |
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| Main Authors: | , , |
| Format: | Article in Journal/Newspaper |
| Language: | English |
| Published: |
Wiley
1990
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| Subjects: | |
| Online Access: | http://dx.doi.org/10.1111/j.1365-2621.1990.tb01574.x https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1111%2Fj.1365-2621.1990.tb01574.x http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1365-2621.1990.tb01574.x/fullpdf |
| Summary: | ABSTRACT Trypsin (EC 3.4.21.4) was isolated from the pyloric ceca of Atlantic cod and purified to homogeneity by affinity chromatography. The enzyme catalyzed the hydrolysis of benzoyl arginine p ‐nitroanilide (BAPA, pH 8.2 and 25°C) such that V max was 250 BAPA units per micromole trypsin and K m was 1.48 mM. For the hydrolysis of tosyl arginine methyl ester (TAME, pH 8.1 and 25°C), V max was 18.2 × 10 3 TAME units/micromole trypsin, and K m 0.22 mM. The pH and temperature optima with BAPA substrate were 7.5 and 40°C, respectively. Atlantic cod trypsin was most active and stable at alkaline pH. The enzyme was heat labile, losing more than 50% of its activity after incubation at 50°C for 30 min. Amino acid analysis of Atlantic cod trypsin revealed that the enzyme was rich in residues such as serine, glycine, glutamate and aspartate, but poor in basic amino acid residues compared to trypsins from warm blooded animals. |
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