Production of new nanobiocatalysts via immobilization of lipase B from C. antarctica on polyurethane nanosupports for application on food and pharmaceutical industries

Nanoflowers: A New Approach of Enzyme Immobilization

“…[7] As an alternative to solve these problems, different immobilization techniques are applied to improve the enzyme stability, specificity, selectivity, ease of recovery, and reuse of enzymes. [8][9][10][11] Furthermore, most standard immobilization techniques lead to significant biocatalyst activity losses compared to free form, lower reaction rates, and additional process costs related to immobilization. [1] To improve biocatalysts' surface area and stability, researchers developed flower-shaped nanostructures.…”

“…Nevertheless, there are limitations to using enzymes on a large scale, such as the biocatalyst‘s high cost and low stability under extreme reaction conditions [7] . As an alternative to solve these problems, different immobilization techniques are applied to improve the enzyme stability, specificity, selectivity, ease of recovery, and reuse of enzymes [8–11] . Furthermore, most standard immobilization techniques lead to significant biocatalyst activity losses compared to free form, lower reaction rates, and additional process costs related to immobilization [1] …”

Hotspots and Mechanisms of Action of the Thermostable Framework of a Microbial Thermolipase

“…However, the reactions catalyzed by lipases are not limited to hydrolysis mentioned above, as they can also perform transesterification and esterification. Furthermore, some lipases exhibiting high thermostability, pH stability, regioselectivity, and enantioselectivity have been widely used in food, , detergent, leather, pharmaceutical, and biodiesel industries. − Hence, novel lipases are being investigated and characterized extensively. Traditional lipases have a lid domain, which exists in open and closed conformations and determines the entry and exit of the substrate during catalysis and a catalytic triad consisting of a nucleophilic serine or cysteine, an aspartic or glutamic acid, and a histidine. , …”

“…However, the reactions catalyzed by lipases are not limited to hydrolysis mentioned above, as they can also perform transesterification and esterification. Furthermore, some lipases exhibiting high thermostability, pH stability, regioselectivity, and enantioselectivity have been widely used in food, 6,7 detergent, leather, 1 pharmaceutical, and biodiesel industries. 8−11 Hence, novel lipases are being investigated and characterized extensively.…”

Effect of Different TiO2 Morphologies on the Activity of Immobilized Lipase for Biodiesel Production

“…Recently, great achievements have been noticed at the synergistic action of biotechnology with nanotechnology by applying modern nanoparticles as a support in the immobilization process. Lipase can be immobilized on different supports such as graphene oxide (GO), iron oxide (Fe 3 O 4 ) nanoparticles, and graphene oxide/iron oxide (GO/Fe 3 O 4 ) nanocomposites, silica aerogel, different types of chitosan, hybrid zinc oxide–iron oxide (ZnOFe) magnetic nanoparticles, polydopamine-coated iron oxide (Fe 3 O 4 _PDA_lipase), flexible nanoporous materials, Cu 3 (PO 4 ) 2 -based inorganic hybrid nanoflower, polyurethane nanosupports, silica magnetic nanoparticles, and titanate and TiO 2 nanoparticles. ,− Nanoparticles are considered as an ideal support in immobilization since they supply better selectivity along with thermal stability, higher enzymatic activity, easy recovery and purification, very small size, large surface area-to-volume ratio, high adsorption ability, and adaptability toward a wider pH range. , Using nanoparticles reduces the diffusion hindrance, leading to the availability of high concentrations of the immobilized biocatalysts compared to the enzymes immobilized onto larger materials.…”