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PROPERTIES OF PHENOLOXIDASE ISOLATED FROM THE CEPHALOTHORAX OF KURUMA PRAWN
( PENAEUS JAPONICUS )
Author(s) -
BENJAKUL SOOTTAWAT,
VISESSANGUAN WONNOP,
TANAKA MUNEHIKO
Publication year - 2005
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2005.00042.x
Subject(s) - cephalothorax , prawn , chemistry , penaeus , trypsin , enzyme assay , copper , enzyme , sodium dodecyl sulfate , biochemistry , fishery , biology , shrimp , organic chemistry , crustacean
Phenoloxidase (PO) from the kuruma prawn cephalothorax was partially purified and characterized. The enzyme showed maximal activity at pH 6.5 and 35C. It was stable in a wide pH range of 3–10 but unstable at a temperature greater than 50C. On the basis of activity staining with L‐β‐(3,4‐dihydroxylphenyl)alanine, the apparent molecular weight was estimated to be 160 kDa. Sodium dodecyl sulfate, methanol and trypsin showed no effect on PO activity, suggesting that the enzyme was isolated in the active form. Phenylthiourea, a copper‐chelating agent, and cysteine exhibited the inhibitory activity against PO in a concentration‐dependent manner. However, copper acetate addition had no influence on the activity.