ArticleApplied biochemistry and biotechnology2025
Further Characterization of Lipase B from Ustilago maydis Expressed in Pichia pastoris: a Member of the Candida antarctica Lipase B-like Superfamily.
Article in Applied biochemistry and biotechnology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Lipases from the basidiomycete fungus Ustilago maydis are promising but underexplored biocatalysts due to their high homology with Candida antarctica lipases. This study provides a comprehensive characterization of a recombinant CALB-like lipase from U. maydis, expressed in Pichia pastoris (rUMLB), and compares its properties with those of the well-studied recombinant lipase B from C. antarctica (rCALB). Biochemical analyses included evaluations of optimal pH, temperature, triglyceride (TG) preference for short- and medium-chain acyl groups, phospholipase and amidase activities, enantiopreference, thermostability, stability in organic solvents, and response to NaCl concentrations. rUMLB, a glycosylated enzyme with a molecular weight of 38.6 kDa, exhibited cold-active behavior at 0 °C and preferred hydrolysis of partially soluble short-chain fatty acid TGs, like rCALB. In addition, rUMLB was also capable of hydrolyzing insoluble long-chain triglycerides like rCALB. The half-life at 50 °C for rCALB was approximately 1.6 times greater than that of UMLB, which has fewer surface-exposed proline residues. Both enzymes displayed strong (R)-enantiopreference on (R)-glycidyl butyrate, (R)-ethyl hydroxy butyrate, and (R)-methyl hydroxy valerate enantiomers with increased activity in non-polar solvents. However, rUMLB was more sensitive to polar solvents. Notably, rUMLB was activated at high NaCl concentrations, as previously reported for rCALB. rUMLB showed amidase activity on capsaicinoids similar to rCALB; however, rUMLB uniquely demonstrated significant phospholipase activity toward natural phospholipids, a feature not observed in rCALB. The analysis of the cavity adjacent to the active site in the UMLB model and CALB structure revealed slightly larger area, volume, and hydrophobicity values for UMLB. These comparative insights highlight the functional diversity within the CALB-type lipase family, underscoring the potential of UMLB as a versatile biocatalyst and providing valuable information for biotechnological applications and for understanding enzyme structure-function relationships within the CALB superfamily.
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