Crab digestive phospholipase: a new invertebrate member.
Crab digestive phospholipase (CDPL) was purified from the hepatopancreas of Carcinus mediterraneus crabs. Homogeneous enzyme was obtained after two chromatography steps: anion exchange and size exclusion HPLC column. Homogeneous CDPL has a molecular mass of 14 kDa as determined by SDS/PAGE analysis. Unlike known digestive phospholipases like porcine PLA(2) (PPPL), CDPL displayed its maximal activity at 50 degrees C and not at 37 degrees C. A specific activity of 40 U/mg for the purified CDPL was measured using PC as substrate under optimal conditions (pH 8 and 50 degrees C) in the presence of 8 mM sodium deoxycholate (NaDC) and 10 mM CaCl(2). In contrast to PPPL, purified CDPL was completely inactivated at 60 degrees C. The N-terminal sequence was determined by automatic Edman degradation. No similarity between 12 N-terminal amino acid residues of CDPL was found with those of known digestive phospholipases. CDPL appears to be a new member of invertebrate phospholipases, and it is potentially useful for treat phospholipid-rich industrial effluents, or to synthesize useful chemical compounds which can be used in the food industry.
Cherif
Slim
S
Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS route de Soukra, 3038 Sfax, Tunisia. slimcherif_enis@yahoo.fr
Ben Bacha
Abir
A
Ben Ali
Yassine
Y
Horchani
Habib
H
Rekik
Wiem
W
Gargouri
Youssef
Y
D000818:Animals; D033364:Decapoda / Q000201:enzymology*; D004789:Enzyme Activation; D004795:Enzyme Stability; D010179:Pancreas / Q000201:enzymology*; D010740:Phospholipases / Q000737:chemistry* / Q000302:isolation & purification*
D010740:Phospholipases