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Parametric study of immobilized cellulase-polymethacrylate particle for the hydrolysis of carboxymethyl cellulose
- Chan, Yi Wei, Acquah, Caleb, Obeng, Eugene M., Dullah, Elvina C., Jeevanandam, Jaison, Ongkudon, Clarence M.
- Biochimie 2019 v.157 pp. 204-212
- Fourier transform infrared spectroscopy, biocatalysts, biocompatibility, carboxymethylcellulose, endo-1,4-beta-glucanase, enzyme activity, ethylenediamines, glutaraldehyde, hydrolysis, immobilized enzymes, industrial applications, models, pH, polymethylmethacrylate
- 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.