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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Bibliographic Details
Published inJournal of food science Vol. 58; no. 4
Main Authors Dionysius, D.A, Hoek, K.S, Milne, J.M, Slattery, S.L
Format Journal Article
LanguageEnglish
Published 01.07.1993
Subjects
CANGREJO DE MAR
CRABE
FOIE
HIGADO
PANCREAS
PROTEASAS
PROTEASE
PURIFICACION
PURIFICATION
TRIPSINA
TRYPSINE
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Summary: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
Bibliography:9429172
Q04
Q02
ISSN:0022-1147
1750-3841
DOI:10.1111/j.1365-2621.1993.tb09357.x