Stability of Burkholderia cepacia Lipase Immobilized on Styrene-Divinylbenzene Activated with Glutaraldehyde, Triton X-100, and Polyethylene Glycol for the Green Synthesis of Hexyl Acetate

戊二醛、Triton X-100 和聚乙二醇活化的固定在苯乙烯-二乙烯基苯上的洋葱伯克霍尔德菌脂肪酶的稳定性及其在己基乙酸酯绿色合成中的应用

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Abstract

This work focuses on improving the stability of Burkholderia cepacia lipase immobilized on styrene-divinylbenzene by using chemical additives and a cost-effective physical adsorption method. Ethanol pretreatment of the supports proved essential for maintaining enzyme activity. The optimal conditions for immobilization were achieved at a 1:1 support-to-enzyme ratio, pH 8, 200 rpm, and 60 °C. Combinations of the additives glutaraldehyde, polyethylene glycol 1500, and Triton X-100 were examined for activation treatment of supports before immobilization. Concentrations of 2.5% (w/v) of polyethylene glycol 1500 and 0.5% (v/v) of Triton X-100 were used to maximize biocatalyst activity. We show that the activated biocatalyst yielded up to 950% more hexyl acetate than non-activated control after 12 reaction cycles. Fourier transform infrared spectroscopy and scanning electron microscopy confirmed the effective immobilization of the Burkholderia cepacia lipase. This study introduces a scalable and sustainable method for creating robust biocatalysts aimed at producing value-added chemicals, thereby advancing green chemistry in the flavor industry.

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