Department of Organic Chemistry and Oil, Faculty of Chemistry, Shahid Beheshti University, Tehran, Iran.
Nanobiotechnology Research Center, Avicenna Research Institute, ACECR, Tehran, Iran.
Bioprocess Biosyst Eng. 2022 Dec;45(12):2043-2060. doi: 10.1007/s00449-022-02808-7. Epub 2022 Nov 10.
The capability of multi-component reactions in rapid immobilization of enzymes was considered for co-immobilization of Thermomyces lanuginous lipase (TLL) and Candida antarctica lipase B (CALB) [TLL: CALB]; Rhizomucor miehei lipase (RML) and CALB [RML: CALB] on amine-functionalized silica-coated magnetic nanoparticles (FeO@SiO-NH). Immobilization of different ratios of lipases was performed within 3 h under mild conditions; producing specific activity ranging from 29 to 35 U/mg for TLL:CALB and 21-34 U/mg for RML:CALB. The co-immobilized derivatives showed improved co-solvent and thermal stability compared to the corresponding free enzymes. All the derivatives were also used to catalyze the transesterification of waste cooking oil with methanol to produce biodiesel (fatty acid methyl esters). Response surface method (RSM) and a central composite rotatable design (CCRD) were used to study the effects of different factors on the FAME yield. FeO@SiO-NH-RML-CALB and FeO@SiO-NH-TLL-CALB had maximum FAME yields of 99-80%, respectively.
多组分反应在快速固定化酶方面的能力被认为可用于Thermomyces lanuginosus 脂肪酶(TLL)和 Candida antarctica 脂肪酶 B(CALB)[TLL:CALB];Rhizomucor miehei 脂肪酶(RML)和 CALB [RML:CALB]的共固定化,在温和条件下,3 小时内完成不同比例脂肪酶的固定化,产生的比活度范围为 29-35 U/mg 的 TLL:CALB 和 21-34 U/mg 的 RML:CALB。与相应的游离酶相比,共固定化衍生物表现出更好的共溶剂和热稳定性。所有衍生物还用于催化废烹饪油与甲醇的酯交换反应,以生产生物柴油(脂肪酸甲酯)。响应面法(RSM)和中心组合旋转设计(CCRD)用于研究不同因素对 FAME 产率的影响。FeO@SiO-NH-RML-CALB 和 FeO@SiO-NH-TLL-CALB 的 FAME 产率最高,分别为 99-80%。