Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa | Zendy

Mahsa Babaei | Zendy; Afzal Karimi | Zendy; Mohammad Amin Hejazi | Zendy

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Use of mesoporous MnO2 as a support for immobilization of lipase from Candida rugosa

Author(s) -

Mahsa Babaei,

Afzal Karimi,

Mohammad Amin Hejazi

Publication year - 2013

Publication title -

chemical industry and chemical engineering quarterly

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.189

H-Index - 26

eISSN - 2217-7434

pISSN - 1451-9372

DOI - 10.2298/ciceq121009019b

Subject(s) - candida rugosa , lipase , rugosa , mesoporous material , chemistry , organic chemistry , biology , catalysis , enzyme , botany

In this study, immobilization of lipase from Candida rugosa on mesoporous manganese dioxide by adsorption method was carried out and the effect of three immobilization variables including temperature, process time and enzyme/support ratio on immobilization efficiency were studied. The characteristics of synthesized MnO2 and lipase-bound MnO2 were investigated by scanning electron microscopy (SEM), transmission electron microscopy (TEM) and Fourier Transform Infrared Spectroscopy (FT-IR) methods. The porous property of the support particles was also studied by X-ray diffraction (XRD) and Brunauer, Emmett, and Teller (BET) measurements. Thermal stability of immobilized lipase was determined to be better than that of free enzyme. Also the operational stability of lipase-bound MnO2 was studied and showed an almost strong attachment of enzyme to support. The Michaelis-Menten kinetic parameters (Km and Vmax) were also determined for both free and immobilized lipases. It was observed that there is an increase of the Km value (672.96 mg/ml) and a decrease of the Vmax value (130.99 U/mg) for the immobilized enzyme comparing with the corresponding values of the free lipase

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