BACKGROUND This work aims to assess the use of protic ionic liquids (PIL), propanoate, butanoate and pentanoate of N‐methylmonoetanolamine (C3, C4 and C5), in the preparation of hybrid supports made of poly(3‐hydroxybutyrate‐co‐hydroxyvalerate) (PHBV) and silica for the immobilization of lipase of Burkholderia cepacia (BCL) by covalent binding. For immobilized biocatalysts (IBs), the performance was determined for immobilization and characterization (pH, temperature, stability thermal, operational and in solvents), with the best conditions being defined. For the supports and efficient IB, the morphological and physicochemical characterization (MEV, BET, FTIR and TGA) was evaluated. RESULTS For preparation of the hybrid support, the experiment using 3 g of PHBV presented a higher percentage of mass, around 50% recovery of the support in the granulometry used. The IBs total activity recovery yield (Ya) in hybrid supports modified with ionic liquids IB‐hybrid‐C3 (103%), IB‐hybrid‐C4 (120%) and IB‐hybrid‐C5 (133%) were above the results reported for the control (90%), with IB‐hybrid‐C5 being the most efficient, and presenting better thermal and operational stability. CONCLUSION Burkholderia cepacia lipase was immobilized successfully in a hybrid support (PHBV and silica) modified with protic ionic liquid by covalent binding, resulting in an improvement in the morphological and physicochemical characteristics, and consequently with greater Ya and good thermal and operational stability. © 2016 Society of Chemical Industry

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Ionic liquids can act as support modifiers and additives in the enzymatic immobilization process, providing more efficient and stable immobilized biocatalysts. In this context, the present work aims to evaluate the influence of aprotic ionic liquids (AIL), ethyl (C2), butyl (C4) e hexyl (C6) of 3-methylimidazolium bis (trifluoromethysulphonyl) imid) in the preparation of hybrid support formed by hydroxybutyrate-hydroxyvalerate (PHBV) and silica for posterior immobilization of Burkholderia cepacia lipase (BCL). Biochemical characterization was evaluted pH (4 -8), temperature (37 -75 °C), thermal stability (55 and 65 °C) and operational stability. Immobilized biocatalysts (IB) higher values immobilization yield obtained IB-C4 (171 ± 1%) and IB-C6 (169 ± 3%) higher than the IB-Control (90%). It can be observed that the free and immobilized BCL by covalent binding presented a better hydrolytic activity at neutral pH (7.0) and the temperature of 50 °C, indicating that the modification of the hybrid support with AIL did not interfere in the pH and optimum temperature of the enzyme. In the study of thermal stability, the AIL modified biocatalysts of higher alkyl chains (C4 and C6) were more stable than the control in the higher ranges of the temperatures studied (55 and 65 °C). The reuse of BCL showed similar results for the biocatalysts IB-C4 and IB-C6, which were reused 11 times, maintaining 50% of the initial activity, whereas the control presented only six reuses. Therefore, the use of modified supports with aprotic ionic liquids for enzyme immobilization offers new perspectives for the industry, thus increasing its efficiency, stability and reuse.

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