Lipase from neon flying squid hepatopancreas: purification and properties

Lipase from hepatopancreas of the neon flying squid (Ommastrephes bartramii) has been partially purified. The molecular weight determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis was 33 000. Optimum pH was around 7.0 and the enzyme was relatively stable between pH 6.0 and 9.0 for 6 h at 25 °C. Optimum temperature of the enzyme reaction was around 25 °C. The enzyme was tolerably stable up to 37 °C. Several triglyceride (TG) molecular species were used as substrates for investigating the positional and fatty acid specificities of the enzyme. With respect to the hydrolysate of TG, the enzyme examined was not an sn-1,3 or an sn-2 positionally specific lipase. The enzyme appeared to have specific activity on monounsaturated and saturated chain TGs, most likely oleic and/ or palmitic acid. In this study, colipase was also separated from the enzyme.