Catalytically active inclusion bodies of cold-adapted lipase: production and its industrial potential.

ABSTRACT: Heterologous overexpression of certain recombinant proteins in E. coli often triggers the formation of inclusion bodies (IBs). Traditionally viewed as inactive aggregates, IBs are now known to sometimes retain native-like folding and catalytic activity, termed catalytically active inclusion bodies (CatIBs). In this work, we investigated the CatIBs formed by recombinant LipAMS8, a cold-adapted lipase from an Antarctic Pseudomonas sp., expressed in E. coli iBL21(DE3)/pET32b. Overexpression yielded abundant insoluble aggregates which were gently isolated using 50 mM Tris-HCl, 50 mM NaCl, 1% Triton X-100 (pH 8.0), and subsequently solubilized in Tris-HCl (pH 8.0) without denaturants. Scanning electron microscopy revealed rod-like protein particles ranging from ~ 100 nm up to 1 μm. Biochemical

SUBMITTER: Bello MN 

PROVIDER: S-EPMC12569326 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature