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Partial protease activity characterization of squid (Todaropsis eblanae) mantle / Caracterización parcial de la actividad proteolítica del manto de pota (Todaropsis eblanae)

Instituto del Frío (CSIC) Ciudad Universitaria s/n, 28040 Madrid, Spain

H. An

Oregon State University-Seafood Laboratory, 2001 Marine Dr, RM 253, Astoria, OR 97103-3427, USA

M.C. Gómez-Guillén

Instituto del Frío (CSIC) Ciudad Universitaria s/n, 28040 Madrid, Spain

P. Montero

Instituto del Frío (CSIC) Ciudad Universitaria s/n, 28040 Madrid, Spain

A.J. Borderías

Instituto del Frío (CSIC) Ciudad Universitaria s/n, 28040 Madrid, Spain

Proteolytic activity in mantle of Todaropsis eblanae was maximum at 40 and 65 °C. Several peaks of activity were detected over the pH range studied (1.5-9.5), indicating the presence of acidic, neutral and alkaline proteases, depending on the temperature. The substantial enzymic inhibition at acidic pH by the inhibitor trans-epoxysuccinyl-L-leucylamine-4-guanidine butane (E-64) revealed the pre dominance of lysosomal cysteine proteases (cathepsins) which showed higher activity at 65 °C than at 40 °C. At 65 °C and pH 5.5 metallo-proteases were also detected by the inhibition with phenanthroline. Serine protease activity predominated at neutral pH (higher at 40 °C than at 65 °C), and cysteine proteases were detected at alkaline pH. There was evidence of cathepsin B and L activity at 65 °C and to a lesser degree at 40 °C.

Key Words: squid • Todaropsis eblanae • proteases • inhibitors

Food Science and Technology International, Vol. 5, No. 5, 391-396 (1999)
DOI: 10.1177/108201329900500504


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