Biocarriers are pivotal in enhancing the reusability of biocatalyst that would otherwise be less economical for industrial application. Ever since the induction of enzymatic technology, varied materials have been assessed for their biocompatibility with enzymes of distinct functionalities. Herein, cellulase was immobilized onto polymethacrylate particles (ICP) as the biocarrier grafted with ethylenediamine (EDA) and glutaraldehyde (GA). Carboxymethyl cellulose (CMC) was used as a model substrate for activity assay. Enzyme immobilization loading was determined by quantifying the dry weight differential of ICP (pre-& post-immobilization). Cellulase was successfully demonstrated to be anchored upon ICP and validated by FTIR spectra analysis. The optimal condition for cellulase immobilization was determined to be pH 6 at 20 °C. The maximum CMCase activity was achieved at pH 5 and 50 °C. Residual activity of ∼50% was retained after three iterations and dipped to ∼18% on following cycle. Also, ICP displayed superior pH adaptability as compared to free cellulase. The specific activity of ICP was 65.14 ± 1.11% relative to similar amount of free cellulase.

生物载体在增强生物催化剂的可重复使用性方面起着至关重要的作用，否则对于工业应用而言，生物催化剂的经济性将降低。自从引入酶促技术以来，已经评估了各种材料与具有不同功能的酶的生物相容性。在此，将纤维素酶作为接枝了乙二胺（EDA）和戊二醛（GA）的生物载体固定在聚甲基丙烯酸酯颗粒（ICP）上。羧甲基纤维素（CMC）用作活性测定的模型底物。通过定量ICP（固定前和固定后）的干重差来确定酶的固定负载量。纤维素酶已成功证明可固定在ICP上，并通过FTIR光谱分析进行了验证。确定纤维素酶固定的最佳条件是在20°C下pH为6。在pH 5和50°C下获得了最大的CMCase活性。经过三次迭代后，残留活性约为50％，并在随后的循环中下降至约18％。而且，与游离纤维素酶相比，ICP表现出优异的pH适应性。相对于类似量的游离纤维素酶，ICP的比活为65.14±1.11％。