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Pinsirodom P, Parkin KL: Selectivity of celite-immobilized patatin (lipid acyl hydrolase) from potato (Solanum tuberosum L.) tubers in esterification reactions As influenced by water activity and glycerol analogues as alcohol acceptors. J Agric Food Chem. 2000 Feb;48(2):155-60.
Lipid acyl hydrolase (LAH; patatin) was purified from potato tubers by ammonium sulfate fractionation followed by anion-exchange and affinity chromatography. The major protein band of 40-43 kDa on SDS-PAGE appeared to be patatin, and it stained positive for lipase activity on native PAGE. Selectivity of a Celite-immobilized potato LAH in esterification reactions with n-acyl fatty acids (FA; C4, C6, C8, C10, C12, C14, C16, and C18) and alcohol acceptors (n-propanol, 2-propanol, 1,3-propanediol, and glycerol; 1,2-propanediol was not sufficiently reactive) was studied in isooctane. Immobilized LAH was highly selective for medium chain FAs (C8/C10) with a secondary optimum for chain lengths of C14/16. Water activity (a (w)) influenced activity and FA selectivity of the enzyme. Initial rates of ester synthesis were greatest at a (w) of 0.90 for all alcohol acceptors except for glycerol, where greatest initial rates were observed at a (w) of 0.19. Immobilized LAH preparations exhibited a bell-shape pH profile with optimum activity at pH 6-7 for ester synthesis, and no effect of pH on FA selectivity was observed. |
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