Abstract
An extracellular alkalophiliclipase was partially purified from heterotrophic Shewanella algae (KX 272637) associated with marine macroalgae Padina gymnospora. The enzyme possessed a molecular mass of 20kD, and was purified 60-fold with a specific activity of 36.33U/mg. The enzyme exhibited Vmax and Km of 1000mM/mg/min and 157mM, respectively, with an optimum activity at 55°C and pH10.0. The catalytic activity of the enzyme was improved by Ca2+ and Mg2+ ions, and the enzyme showed a good tolerance towards organic solvents, such as methanol, isopropanol, and ethanol. The purified lipase hydrolyzed the refined liver oil fromleafscale gulper shark Centrophorus squamosus, yielding a total C20-22 n-3 PUFA concentration of 34.99% with EPA+DHA accounting the major share (34% TFA), after 3h of hydrolysis. This study recognized the industrial applicability of the thermostable and alkalophilic lipase from marine macroalga-associated bacterium Shewanella algae to produce enriched C20-22 n-3 polyunsaturated fatty acid concentrate.
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