Bebić Jelena, Banjanac Katarina, Rusmirović Jelena, Ćorović Marija, Milivojević Ana, Simović Milica, Marinković Aleksandar, Bezbradica Dejan
Directorate of Measures and Precious Metals Mike Alasa 14 11000 Belgrade Serbia.
Innovation Centre of Faculty of Technology and Metallurgy, University of Belgrade Karnegijeva 4 11000 Belgrade Serbia
RSC Adv. 2020 Jun 4;10(36):21495-21508. doi: 10.1039/d0ra03439h. eCollection 2020 Jun 2.
In this research, it has been demonstrated that amino-modified microspheres (A-LMS) based on bio-waste derived material, such as kraft lignin, have good prospects in usage as a support for enzyme immobilization, since active biocatalyst systems were prepared by immobilizing β-galactosidase from and laccase from expressed in (Novozym® 51003) onto A-LMS. Two types of A-LMS were investigated, with different emulsifier concentrations (5 wt% and 10 wt%), and microspheres produced using 5 wt% of emulsifier (A-LMS_5) showed adequate pore shape, size and distribution for enzyme attachment. The type of interactions formed between enzymes (β-galactosidase and laccase) and A-LMS_5 microspheres demonstrated that β-galactosidase is predominantly attached electrostatic interactions while attachment of laccase is equally governed by electrostatic and hydrophobic interactions. Furthermore, the A-LMS_5-β-galactosidase exhibited specificity towards recognized prebiotics (galacto-oligosaccharides (GOS)) synthesis with 1.5-times higher GOS production than glucose production, while for environmental pollutant lindane degradation, the immobilized laccase preparation exhibited high activity with a minimum remaining lindane concentration of 22.4% after 6 days. Thus, this novel enzyme immobilization support A-LMS_5 has potential for use in green biotechnologies.
在本研究中,已证明基于生物废弃物衍生材料(如硫酸盐木质素)的氨基修饰微球(A-LMS)作为酶固定化载体具有良好的应用前景,因为通过将源自[具体来源未提及]的β-半乳糖苷酶和源自[具体来源未提及]且在[具体宿主未提及]中表达的漆酶(诺维信®51003)固定在A-LMS上制备了活性生物催化剂系统。研究了两种不同乳化剂浓度(5 wt%和10 wt%)的A-LMS,使用5 wt%乳化剂制备的微球(A-LMS_5)显示出适合酶附着的孔形状、尺寸和分布。酶(β-半乳糖苷酶和漆酶)与A-LMS_5微球之间形成的相互作用类型表明,β-半乳糖苷酶主要通过静电相互作用附着,而漆酶的附着则同样受静电和疏水相互作用的支配。此外,A-LMS_5-β-半乳糖苷酶对公认的益生元(低聚半乳糖(GOS))合成具有特异性,其GOS产量比葡萄糖产量高1.5倍,而对于环境污染物林丹的降解,固定化漆酶制剂表现出高活性,6天后林丹的最低残留浓度为22.4%。因此,这种新型酶固定化载体A-LMS_5具有在绿色生物技术中应用的潜力。