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Phenoloxidase from the Cuticle of Florida Spiny Lobster ( Panulirus argus ): Mode of Activation and Characterization
Author(s) -
FERRER OBDULIO J.,
KOBURGER JOHN A.,
OTWELL W. STEVEN,
GLEESON RICK A.,
SIMPSON BENJAMIN K.,
MARSHALL MAURICE R.
Publication year - 1989
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.1989.tb08568.x
Subject(s) - spiny lobster , panulirus argus , cuticle (hair) , trypsin , enzyme , substrate (aquarium) , chemistry , incubation , crustacean , biochemistry , biology , anatomy , zoology , ecology
Phenoloxidase (PO) from lobster cuticle existed as a large inert enzyme (IPO1) which became active (15‐fold increase) upon incubation at 4°C and 3 days storage. Electrophorcsis of day 3 extracts showed that the large enzyme disappeared gradually while a new PO (EAPO) developed (Mw of 62.5 kDA). Trypsin treatment yielded a similar enzyme (TAPO2; 64 kDA). Kinetic properties such as Km and E a indicated that dihydroxyphenylalanine (DOPA) appeared to be a more physiologically important substrate for the trypsin treated PO than EAPO. In addition, temperature and pH properties indicated that different structural and functional properties existed between the three forms (IPO1, EAPO, TAPO2).