Abstract

Detergent-stable proteases were found in crude extract of the Antarctic scallop Adamussium colbecki. The results of gelatin zymography indicated the availability of the proteases which able to act in the presence of SDS, whereas plasmin and miniplasmin maintained their activity toward gelatin only after complete removing of detergent. Total proteolytic activity, represented by casein hydrolysis was within the control level after incubation of crude extract with detergents such as Tween 80 and SDS whereas trypsin activity was significantly reduced.

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