Correa Wellington M, Osório Wislei R, Bortolozo Ausdinir D, Poloni Erik, Padilha Giovana S
Centro de Pesquisa em Manufatura e Materiais Avançados, Faculdade de Ciências Aplicadas, Universidade Estadual de Campinas (Unicamp), Limeira, SP, 13484-350, Brazil.
Faculdade de Tecnologia, Universidade Estadual de Campinas (Unicamp), Limeira, SP, 13484-332, Brazil.
Appl Biochem Biotechnol. 2025 Jun 4. doi: 10.1007/s12010-025-05277-2.
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.
本研究聚焦于通过使用化学添加剂和一种经济高效的物理吸附方法,提高固定在苯乙烯-二乙烯基苯上的洋葱伯克霍尔德菌脂肪酶的稳定性。载体的乙醇预处理被证明对维持酶活性至关重要。固定化的最佳条件是载体与酶的比例为1:1、pH值为8、转速为200转/分钟以及温度为60°C。在固定化之前,研究了戊二醛、聚乙二醇1500和吐温X-100等添加剂组合对载体的活化处理。使用2.5%(w/v)的聚乙二醇1500和0.5%(v/v)的吐温X-100浓度来最大化生物催化剂活性。我们发现,经过12个反应循环后,活化后的生物催化剂产生的乙酸己酯比未活化的对照多950%。傅里叶变换红外光谱和扫描电子显微镜证实了洋葱伯克霍尔德菌脂肪酶的有效固定。本研究介绍了一种可扩展且可持续的方法,用于制备旨在生产高附加值化学品的强大生物催化剂,从而推动香料行业的绿色化学发展。