# 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

## TL;DR

Researchers improved the stability of a bacterial enzyme used to make a flavor chemical, achieving high efficiency through a green chemistry method.

## Contribution

A scalable and sustainable method for immobilizing Burkholderia cepacia lipase with enhanced stability and activity is introduced.

## Key findings

- Ethanol pretreatment of supports was essential for maintaining enzyme activity during immobilization.
- The activated biocatalyst produced up to 950% more hexyl acetate than the non-activated control after 12 cycles.
- FTIR and SEM confirmed successful immobilization of the enzyme on the support material.

## 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.