Partial characterization of pyloric-duodenal lipase of gilthead seabream (Sparus aurata).
In the present study, we report the isolation and characterization of seabream Sparus aurata pyloric caeca-duodenal lipase. Optimum activity was found at pH 8.5 and salinity of 50 mM NaCl. Lipase activity was sensitive to divalent ions, and extreme pH values (4, 5, and 12), being more stable at alkaline than acid pH. Optimum temperature was found at 50°C, but lipase was stable at temperatures below 40°C. Lipase has a bile salt sodium taurocholate requirement for increased activity. Gradient PAGE electrophoresis revealed the presence of four isoforms with apparent molecular masses of 34, 50, 68, and 84 KDa, respectively. Pyloric-duodenal lipase was able to hydrolyze emulsified alimentary oils. Results confirm the presence of true lipases in Sparus aurata digestive tract.
Nolasco
Héctor
H
Centro de Investigaciones Biológicas del Noroeste, S.C., Mar Bermejo No. 195, Col. Playa Palo Santa Rita, La Paz, BCS, Mexico. hnolasco04@cibnor.mx
Moyano-López
Francisco
F
Vega-Villasante
Fernando
F
D000818:Animals; D002413:Cations, Divalent / Q000494:pharmacology; D004386:Duodenum / Q000201:enzymology*; D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D005753:Gastric Mucosa / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008049:Lipase / Q000302:isolation & purification / Q000378:metabolism*; D000069463:Olive Oil; D010938:Plant Oils / Q000378:metabolism; D020033:Protein Isoforms; D021541:Sea Bream / Q000502:physiology*; D012965:Sodium Chloride / Q000494:pharmacology; D013656:Taurocholic Acid / Q000494:pharmacology; D013696:Temperature
D002413:Cations, Divalent; D000069463:Olive Oil; D010938:Plant Oils; D020033:Protein Isoforms; D012965:Sodium Chloride; D013656:Taurocholic Acid; D008049:Lipase