| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 49646 | Catalysis Communications | 2015 | 4 Pages |
•Enzymatic production of d-sorbitol monoesters with various fatty acids was studied.•Substrate specificities of Candida sp. 99–125 were compared.•Pretreatment significantly facilitated the equilibrium.•Excellent surface properties were demonstrated.
Sugar fatty acid esters are surfactants that are widely used in food, cosmetics, and pharmaceutical industries. In this study, enzymatic production of d-sorbitol monoesters with various fatty acids (C10–C18) was assessed. Reactions were performed in tert-butanol at 40 °C, catalyzed by Candida sp. 99–125 lipase. Dissolution of the substrates was found to be the limiting step of the reaction, and hence preheating was performed to increase the solubility of d-sorbitol. Thus, the yield of d-sorbitol palmitate was increased from 7.34 to 31.6 mM. The results demonstrated that the specific lipase preferred long-chain fatty acids. The surface-active properties of the products were also determined.
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