Bifunctional carbohydrate biopolymers entrapped lipase as catalyst for the two consecutive conversions of α-pinene to oxy-derivatives

Bifunctional catalysts designed as carbohydrate biopolymers entrapping lipase have been investigated for the biotransformation of a natural compound (alpha-pinene) to oxy-derivatives. Lipases assisted the epoxidation of alpha-pinene using H2O2 as oxidation reagent and ethyl acetate as both acetate-supplier and solvent affording alpha-pinene oxide as the main product. Further, the biopolymer promoted the isomerization of alpha-pinene oxide to campholenic aldehyde and trans-carenol. In this case, the biopolymers played double roles of the support and also active part of the bifunctional catalyst. Screening of enzymes and their entrapping in a biopolymeric matrix (e.g. Ca-alginate and kappa-carrageenan) indicated the lipase extracted from Aspergillus niger as the most efficient. In addition, the presence of biopolymers enhanced the catalytic activity of the immobilized lipase (i.e. 13.39 x 10(3), 19.76 x 10(3)and 26.46 x 10(3) for the free lipase, lipase-carrageenan and lipase-alginate, respectively). The catalysts stability and reusability were confirmed in eight consecutively reaction runs. (C) 2016 Elsevier Ltd. All rights reserved.