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The positional selectivity of several commercial lipases was reevaluated from the point of view of synthetic utility. A 1,2‐diglyceride was synthesized, and exposed to typical conditions of lipase‐catalyzed hydrolysis (without the enzyme). Little, or no, acyl migration was observed. The recovery of oleic acid from several lipase‐catalyzed hydrolyses of 1(3)‐palmitoyl‐2‐oleoyl‐3(1)‐stearoyl glycerol (POS) reported here, therefore, must be regarded as due to the presence of the lipases themselves. This could limit the use of such catalysts in schemes requiring high selectivity for the primary positions of triglycerides. Fatty acid selectivity data of the enzymes studied also are presented.

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