Trypsin-like enzyme from sand crab (Portunus pelagicus): purification and characterization
Studies with synthetic substrates and specific inhibitors indicated that a proteinase from the hepatopancreas of the sand crab (Portunus pelagicus) was a trypsin like serine proteinase. The molecular weight of the enzyme estimated by gel filtration and mass spectrometry was 25,000, whereas SDS-PAGE...
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| Published in | Journal of food science Vol. 58; no. 4 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
| Published |
01.07.1993
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| Subjects | |
| Online Access | Get more information |
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| Abstract | Studies with synthetic substrates and specific inhibitors indicated that a proteinase from the hepatopancreas of the sand crab (Portunus pelagicus) was a trypsin like serine proteinase. The molecular weight of the enzyme estimated by gel filtration and mass spectrometry was 25,000, whereas SDS-PAGE indicated a molecular weight of 34,800. The optimum temperature for hydrolysis of azocasein was 60 degrees C, while inactivation of 50% enzymic activity occurred at 68 degrees C. The enzyme, optimally active at pH 8.0 towards p-tosyl-L-arginine methyl ester and unstable at acid pH, was high in acidic amino acid residues. Under some conditions the enzyme readily autodigested. Our results can help understand and avoid problems of meat softening during storage of seafood products |
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| AbstractList | Studies with synthetic substrates and specific inhibitors indicated that a proteinase from the hepatopancreas of the sand crab (Portunus pelagicus) was a trypsin like serine proteinase. The molecular weight of the enzyme estimated by gel filtration and mass spectrometry was 25,000, whereas SDS-PAGE indicated a molecular weight of 34,800. The optimum temperature for hydrolysis of azocasein was 60 degrees C, while inactivation of 50% enzymic activity occurred at 68 degrees C. The enzyme, optimally active at pH 8.0 towards p-tosyl-L-arginine methyl ester and unstable at acid pH, was high in acidic amino acid residues. Under some conditions the enzyme readily autodigested. Our results can help understand and avoid problems of meat softening during storage of seafood products |
| Author | Slattery, S.L Milne, J.M Hoek, K.S Dionysius, D.A |
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| CitedBy_id | crossref_primary_10_1111_j_1745_4514_2001_tb00743_x crossref_primary_10_1007_s10989_007_9119_7 crossref_primary_10_1007_s00360_008_0263_y crossref_primary_10_1016_j_cbpc_2004_03_002 crossref_primary_10_1111_j_1745_4514_2000_tb00695_x crossref_primary_10_1111_j_1745_4514_2000_tb00699_x crossref_primary_10_1007_s11033_011_0915_y crossref_primary_10_1080_10498850_2018_1449154 crossref_primary_10_1007_s10068_012_0147_5 crossref_primary_10_3354_ab00396 crossref_primary_10_1016_S0305_0491_00_00183_8 crossref_primary_10_1016_j_cbpb_2007_08_008 crossref_primary_10_1111_j_1365_2109_2009_02183_x |
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| Title | Trypsin-like enzyme from sand crab (Portunus pelagicus): purification and characterization |
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