Biochemical and physical characterization of immobilized Candida rugosa lipase on metal oxide hybrid support

• Main Authors: Ramlee, Nurfadhila Nasya, Md. Illias, Rosli, A. Rahman, Roshanida, Toemen, Susilawati, Selvasembian, Rangabhashiyam, Ahmad, Rabi’atul Adawiyah, Abdul Manas, Nor Hasmaliana, Wan Azelee, Nur Izyan
• Format: Article
• Language: English
• Published: MDPI 2022
• Subjects: TP Chemical technology
• Online Access: http://eprints.utm.my/id/eprint/101344/1/NurIzyanWanAzelee2022_BiochemicalandPhysicalCharacterizationofImmobilizedCandidaRugosa.pdf; http://eprints.utm.my/id/eprint/101344/; http://dx.doi.org/10.3390/catal12080854

Enzyme immobilization on inorganic materials is gaining more attention with the potential characteristics of high-surface-area-to-volume ratios, increasing the efficiency of enzyme loading on the support. Metal oxide hybrid support was prepared by a wetness impregnation of five metal precursors, including CaO, CuO, MgO, NiO, and ZnO, on Al2O3 and used as a support for the immobilization of Candida rugosa lipase (CRL) by adsorption. Maximum activity recovery (70.6%) and immobilization efficiency (63.2%) were obtained after optimization of five parameters using response surface methodology (RSM) by Box–Behnken design (BBD). The biochemical properties of immobilized CRL showed high thermostability up to 70 °C and a wide range in pH stability (pH 4–10). TGA-DTA and FTIR analysis were conducted, verifying thermo-decomposition of lipase and the presence of an amide bond. FESEM-EDX showed the homogeneous distribution and high dispersion of magnesium and CRL on MgO-Al2O3, while a nitrogen adsorption–desorption study confirmed MgO-Al2O3 as a mesoporous material. CRL/MgO-Al2O3 can be reused for up to 12 cycles and it demonstrated high tolerance in solvents (ethanol, isopropanol, methanol, and tert-butanol) compared to free CRL.