Electrospun Magnetic Nanocellulose-Polyethersulfone-Conjugated Lipase for Synthesis of Ethyl Valerate.

A novel greener MNC/PES membrane was developed through an electrospinning technique for lipase immobilization to catalyze the synthesis of ethyl valerate (EV). In this study, the covalent immobilization of lipase (AOL) onto an electrospun nanofibrous membrane consisting of magnetic nanocellulose (MNC) and polyethersulfone (PES) to produce EV was statistically optimized. Raman spectroscopy, Fourier-transform infrared spectroscopy: attenuated total reflection, field emission scanning electron microscopy, energy dispersive X-ray spectroscopy, thermal gravimetric analysis (TGA), and differential thermal gravimetric (DTG) of MNC/PES-AOL demonstrated that AOL was successfully immobilized onto the fibers.

Operational Stability, Regenerability, and Thermodynamics Studies on Biogenic Silica/Magnetite/Graphene Oxide Nanocomposite-Activated Lipase.

Inorganic biopolymer-based nanocomposites are useful for stabilizing lipases for enhanced catalytic performance and easy separation. Herein, we report the operational stability, regenerability, and thermodynamics studies of the ternary biogenic silica/magnetite/graphene oxide nanocomposite (SiO/FeO/GO) as a support for lipase (CRL). The X-ray photoelectron spectroscopy (XPS), X-ray diffraction (XRD), field-electron scanning electron microscopy (FESEM), vibrating sample magnetometry (VSM), and nitrogen adsorption/desorption data on the support and biocatalyst corroborated their successful fabrication.

Ternary biogenic silica/magnetite/graphene oxide composite for the hyperactivation of Candida rugosa lipase in the esterification production of ethyl valerate.

Oil palm leaves (OPL) silica (SiO) can replace the energy-intensive, commercially produced SiO. Moreover, the agronomically sourced biogenic SiO is more biocompatible and cost-effective enzyme support, which properties could be improved by the addition of magnetite (FeO) and graphene oxide (GO) to yield better ternary support to immobilize enzymes, i.e.