Immobilized inclusion bodies of recombinant cold-adaptive lipase from Antarctic Pseudomonas sp. as catalysts.

ABSTRACT: Immobilization of lipase has been receiving attention for a long time; this is because of the need for robust catalysts by industries. Numerous literature has reported improvements in the properties of immobilized lipase in terms of stability when exposed to extreme conditions of temperature, pH, and organic solvents commonly encountered in most industrial settings. However, some microbial lipases that have the potential to catalyze significant reactions do occur in the form of inclusion bodies when expressed in Escherichia coli. This research aimed to immobilize catalytically active inclusion bodies (CatIBs) of LipAMS8 lipase onto Seplite LX120 as the adsorption material. Scanning electron microscopy and Fourier infrared spectroscopy were used to ascertain the immobilization. Immobilized

SUBMITTER: Bello MN 

PROVIDER: S-EPMC12535532 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature