Alves Nanda R, Pereira Matheus M, Giordano Raquel L C, Tardioli Paulo W, Lima Álvaro S, Soares Cleide M F, Souza Ranyere L
UNIT, Universidade Tiradentes, Av. Murilo Dantas, 300, Farolândia, Aracaju, SE, Brazil.
Chemistry Department, CICECO, University of Aveiro, Campus Universitário de Santiago Aveiro, 3810-193, Aveiro, Portugal.
Bioprocess Biosyst Eng. 2021 Jan;44(1):57-66. doi: 10.1007/s00449-020-02419-0. Epub 2020 Aug 7.
A new design of cross-linked enzyme aggregates (CLEAs) of Burkholderia cepacia lipase (BCL) based mainly on the use of lignocellulosic residue of palm fiber as an additive was proposed. Different parameters for the preparation of active CLEAs in the hydrolysis of olive oil, such as precipitation agents, crosslinking agent concentration, additives, and coating agents were investigated. The highest activity yield (121.1 ± 0.1%) and volumetric activity (1578.1 ± 2.5 U/mL) were achieved for CLEAs prepared using the combination of a coating step with Triton X-100 and polyethyleneimine plus the use of palm fiber as an additive. The variations of the secondary structures of BCL-CLEAs were analyzed by second-derivative infrared spectra, mainly indicating a reduction of the α-helix structure, which was responsible for the lipase activation in the supramolecular structure of the CLEAs. Thus, these results provided evidence of an innovative design of BCL-CLEAs as a sustainable and biocompatible opportunity for biotechnology applications.
提出了一种新的洋葱伯克霍尔德菌脂肪酶（BCL）交联酶聚集体（CLEAs）设计，主要基于使用棕榈纤维的木质纤维素残渣作为添加剂。研究了在橄榄油水解中制备活性CLEAs的不同参数，如沉淀剂、交联剂浓度、添加剂和包衣剂。使用Triton X-100和聚乙烯亚胺的包衣步骤与使用棕榈纤维作为添加剂相结合制备的CLEAs实现了最高的活性产率（121.1±0.1%）和体积活性（1578.1±2.5 U/mL）。通过二阶导数红外光谱分析了BCL-CLEAs二级结构的变化，主要表明α-螺旋结构减少，这是CLEAs超分子结构中脂肪酶激活的原因。因此，这些结果为BCL-CLEAs作为生物技术应用的可持续和生物相容性机会的创新设计提供了证据。
