A Novel Lipase from Streptomyces exfoliatus DSMZ 41693 for Biotechnological Applications.

ABSTRACT: Genome mining of Streptomyces exfoliatus DSMZ 41693 has allowed us to identify four different lipase-encoding sequences, and one of them (SeLipC) has been successfully cloned and extracellularly expressed using Rhodococcus sp. T104 as a host. SeLipC was purified by one-step hydrophobic interaction chromatography. The enzyme is a monomeric protein of 27.6 kDa, which belongs to subfamily I.7 of lipolytic enzymes according to its phylogenetic analysis and biochemical characterization. The purified enzyme shows the highest activity at 60 °C and an optimum pH of 8.5, whereas thermal stability is significantly improved when protein concentration is increased, as confirmed by thermal deactivation kinetics, circular dichroism, and differential scanning calorimetry. Enzy

SUBMITTER: Rodriguez-Alonso G 

PROVIDER: S-EPMC10707221 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature