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

• 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.

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