Improving catalytic performance of Burkholderia cepacia lipase immobilized on macroporous resin NKA

The lipase from Burkholderia cepacia adsorbed on macroporous resin NKA was investigated by combined strategies of bioimprinting and interfacial activation to enhance its catalytic performance. The specific activity of the derivative lipase was 211,733.3 U/g-protein, which was 21.7-fold, 19.4% and 47% enhancement over the free lipase powder, non-bioimprinted and non-interfacial activation lipase, respectively. The derivative lipase exhibited a satisfactory thermal stability over a wide range of temperature (from 30 °C to 70 °C) and a strong tolerance to organic solvents such as methanol, ethanol and acetone with 50% concentration. After being used of 50 successive batches (400 h), the derivative lipase still retained over 92% of its original activity (methyl esters yield decreased from 98% to 90%). Circular dichroism analysis indicated that the activity enhancement of the derivative lipase was ascribed to the secondary structure changes. The derivative lipase preparation in this work was probably a promising alternative to produce a biocatalyst of satisfactory thermo-stability, strong solvents tolerance and high operational reusability.

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► The combined strategies of immobilization, bioimprinting and interfacial activation were employed to prepare the derivative lipase.
► The performance properties of the derivative lipase of satisfactory thermo-stability, strong solvents tolerance and high operational reusability were elucidated.
► The activity variance of the derivative lipase was ascribed to the variance of its secondary structure via circular dichroism analysis.