Immobilization of Recombinant Endoglucanase (CelA) from Clostridium thermocellum on Modified Regenerated Cellulose Membrane

Cellulases are being widely employed in lignocellulosic biorefineries for the sustainable production of value-added bioproducts. However, high cost, sensitivity, and non-reusability free cellulase enzymes impede their commercial applications. Enzyme immobilization seems to be a potential approach address aforesaid complications. The current study aims at recombinant endoglucanase (CelA) originated from cellulosome Clostridium thermocellum Escherichia coli (E. coli), followed by using modified regenerated cellulose (RC) membranes. surface modification RC membranes was performed two different ways: one generate immobilized metal ion affinity RC-EPI-IDA-Co2+ (IMAMs) coordination coupling another develop aldehyde functional group RC-EPI-DA-GA (AMs) covalent bonding. For preparation IMAMs, cobalt ions expressed highest effect compared other ions. Both enzyme-immobilized exhibited better thermal stability maintained an improved relative activity higher temperatures (50–90 °C). In storage analysis, 80% retained after 15 days 4 °C. Furthermore, IMAM- AM-immobilized CelA 63% 53% activity, respectively, reused five times. As purification during immobilization, IMAMs showed fold 3.19 than AMs. also displayed kinetic parameters, with Vmax 15.57 U mg−1 lower Km 36.14 mg mL−1, those were via treatment stripping buffer reloaded almost 100% same as enzymes, up 5 cycles regeneration.