Strategies to immobilize the individual enzymes are crucial for enhancing catalytic applicability and require a controlled immobilization process. Herein, protocol for immobilizing Candida rugosa lipase (CRL) onto modified magnetic silica derived from oil palm leaves ash (OPLA) was optimized for the effects of concentration of CRL, immobilization time, and temperature, monitored by titrimetric and spectrometric methods. XRD and TGA-DTG spectrometric observations indicated that OPLA-silica was well coated over magnetite (SiO₂-MNPs) and CRLs were uniformly bound by covalent bonds to SiO₂-MNPs (CRL/Gl-A-SiO₂-MNPs). The optimized immobilization protocol showed that in the preparation of CRL/Gl-A-SiO₂-MNPs, CRL with 68.3 mg/g protein loading and 74.6 U/g specific activity was achieved using 5 mg/mL of CRL, with an immobilization time of 12 h at 25 °C. The present work also demonstrated that acid-pretreated OPLA is a potential source of renewable silica, envisioning its applicability for practical use in enzymatic catalysis on solid support.

固定单个酶的策略对于增强催化适用性至关重要，并且需要受控的固定过程。在此，针对滴定念珠菌脂肪酶（CRL）固定在衍生自油棕叶灰分（OPLA）的改性磁性二氧化硅上的方案进行了优化，以通过滴定法和光谱法监测CRL的浓度，固定时间和温度。XRD和TGA-DTG光谱观察表明，OPLA-二氧化硅被良好地覆盖在磁铁矿（SiO ₂ -MNP）上，并且CRL通过共价键均匀地结合到SiO ₂ -MNP（CRL / G1-A-SiO ₂ -MNP）上。优化的固定方案表明，在制备CRL / Gl-A-SiO _2时-MNPs，使用5 mg / mL的CRL，在25°C下固定时间为12 h，可实现68.3 mg / g的蛋白质负载和74.6 U / g的比活性的CRL。本工作还证明了酸预处理的OPLA是可再生二氧化硅的潜在来源，并设想了其在固体载体上的酶催化中的实际应用性。