Silylation of mica for lipase immobilization as biocatalysts in esterification
Source abstract
Abstract
Abstract Mica was modified either by acid treatment, grafting with aminopropyl-, octyl-, vinyl-, mercapto- and glycidoxy-triethoxysilanes, and activation of pre-treated support with glutaraldehyde (Glu). The derivatives were characterized by X-ray diffraction (XRD), infra-red spectroscopy (FTIR), surface area and porosity analysis, scanning electron microscopy coupled with energy dispersive X-ray (SEM-EDX) and transmission electron microscopy (TEM) techniques. The modified micas were used for immobilization of lipase from Candida rugosa (CRL). Activity of the lipase was determined by esterification and exhibited the improved activity than the free enzyme following the order; Amino-CRL > Glu-Amino-CRL > Octyl-CRL > Vinyl-CRL > Glycidoxy-CRL > Mercapto-CRL > Mica-CRL. Lipase immobilized mica showed enhanced protein loading (up to 8.22 mg protein/g support) and immobilization (up to 78%) compared to the free lipase and unmodified mica.
Source: openaire · Quality: candidate unverified · Source record ↗
Research context
OpenAlex topics: Enzyme Catalysis and Immobilization · biodegradable polymer synthesis and properties · Electrochemical sensors and biosensors
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (31)
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