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Isolation and characterization of five serine proteases with trypsin chymotrypsin and elastase like characteristics from the gut of the lugworm arenicola marina l. polychaeta


, : Isolation and characterization of five serine proteases with trypsin chymotrypsin and elastase like characteristics from the gut of the lugworm arenicola marina l. polychaeta. Journal of Comparative Physiology B Biochemical Systemic and Environmental Physiology 162(2): 159-167

Five proteases were isolated from the digestive fluid of the lugworm. Arenicola marina L. The enzymes (molecular weight 24.0-24.6 kDa) were classified as serine proteases. Three enzymes showed a cleavage specificity corresponding to mammalian trypsin (E.C. 3.4.21.4). One protease possessed a chymotrypsin-like cleavage pattern (EC. 3.4.21.1), and the fifth preferred cleavage behind short-chain amino acids like an elastase (E.C. 3.4.21.36). Detailed investigations revealed differences in molecular characteristics and cleavage patterns compared to mammalian proteases, especially in the chymotrypsin- and the elastase-like enzymes.

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