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

[Display omitted] •Bifunctional biocatalyst for consecutive conversion of α-pinene to oxy-derivatives.•Biopolymer playing double role – support and active part of the biocatalyst.•Textural characterization of lipase-biopolymer catalyst based on SEM analysis.•Ca-alginate and κ-carrageenan improved the performance of lipase activity.•Catalysts stability and reusability confirmed in eight consecutively reaction runs. Bifunctional catalysts designed as carbohydrate biopolymers entrapping lipase have been investigated for the biotransformation of a natural compound (α-pinene) to oxy-derivatives. Lipases assisted the epoxidation of α-pinene using H2O2 as oxidation reagent and ethyl acetate as both acetate-supplier and solvent affording α-pinene oxide as the main product. Further, the biopolymer promoted the isomerization of α-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 κ-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. 13.39×103, 19.76×103and 26.46×103 for the free lipase, lipase-carrageenan and lipase-alginate, respectively). The catalysts stability and reusability were confirmed in eight consecutively reaction runs.