Abstract
Immobilization of lipase was successfully achieved on the surface of magnetically separable Fe3O4/graphene oxide (GO) via a post-modification. This post modification was achieved in alternation to glutaraldehyde post-modification. The activity of immobilized lipase had not a significant loss in the activity while on the other hand, it is simply extractable (by keeping its major activity) from reaction crude by a magnet. Each step of immobilization was carefully monitored by characterization and all were successfully proved. SEM, TEM, XRD, EDX, and FTIR were used to characterize the support and immobilization process.
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