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

Abstract

Article Highlights• We used a new mesoporous carrier for immobilization of lipase from Candida rugosa • The amount of enzyme loading on support was reached to 700 units per 1 g of support • The thermal resistance of the enzyme was enhanced by immobilization • The physical adsorption of enzyme to the support was strong Abstract In this study, immobilization of lipase from Candida rugosa on mesoporous manganese dioxide by adsorption 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 MnO 2 and lipase-bound MnO 2 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. The thermal stability of immobilized lipase was determined to be better than that of free enzyme. Also the operational stability of lipase-bound MnO 2 was studied and showed an almost strong attachment of enzyme to support. The Michaelis-Menten kinetic parameters (K m and V max ) were also determined for both free and immobilized lipases. It was observed that there is an increase of the K m value (672.96 mg/ml) and a decrease of the V max value (130.99 U/mg) for the immobilized enzyme comparing with the corresponding values of the free lipase.

Immobilization of Thrombin to Alginate Gel and in vitro Application of Immobilized Thrombin

“…Therefore, enzymes could not work continuously. At the same time, immobilization reaction time should be optimal for the prevention of losing time during the immobilization [22]. The immobilization process should be done as quickly and efficiently as possible.…”

Immobilization of horseradish peroxidase onto electrospun polyurethane nanofiber matrices

“…Details concerning these assays can be found in the Supplementary Material, Item 4. Several authors attributed this effect to the thermal inactivation of enzymes 40–42 . In particular, some authors reported that temperatures higher than 30°C favored the inactivation of free and grafted HRP 17,18,43 .…”

“…Several authors attributed this effect to the thermal inactivation of enzymes. [40][41][42] In particular, some authors reported that temperatures higher than 30 C favored the inactivation of free and grafted HRP. 17,18,43 In conclusion, obtained results demonstrate that immobilization conditions corresponding to MAH95 20 were the most favorable among the tested ones to obtain electrospun nanofiber matrices with high peroxidase activity.…”

Biodiesel Production by Aspergillus niger Lipase Immobilized on Barium Ferrite Magnetic Nanoparticles

“…Lipases (triacylglycerol acyl hydrolases, EC 3.1.1.3) are largely used as biocatalysts in biotechnology and modern chemistry [ 7 ]. These enzymes are also catalyzing several reactions like esterification [ 8 ], transesterification, acidolysis, interesterification, alcoholysis, aminolysis, oximolysis, thiotransesterification and ammoniolysis in anhydrous organic solvents [ 9 ]. Lipase is widely found in animals, plants and microorganisms [ 10 ].…”