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A Novel Lipase from Streptomyces exfoliatus DSMZ 41693 for Biotechnological Applications

Genome mining of DSMZ 41693 has allowed us to identify four different lipase-encoding sequences, and one of them ( LipC) has been successfully cloned and extracellularly expressed using sp. T104 as a host. LipC was purified by one-step hydrophobic interaction chromatography. The enzyme is a monomeri...

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Bibliographic Details
Published in:International journal of molecular sciences 2023-12, Vol.24 (23), p.17071
Main Authors: Rodríguez-Alonso, Guillermo, Toledo-Marcos, Juan, Serrano-Aguirre, Lara, Rumayor, Carlos, Pasero, Beatriz, Flores, Aida, Saborido, Ana, Hoyos, Pilar, Hernáiz, María J, de la Mata, Isabel, Arroyo, Miguel
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Language:English
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Summary:Genome mining of DSMZ 41693 has allowed us to identify four different lipase-encoding sequences, and one of them ( LipC) has been successfully cloned and extracellularly expressed using sp. T104 as a host. LipC 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. Enzyme hydrolytic activity using -nitrophenyl palmitate (pNPP) as substrate can be modulated by different water-miscible organic cosolvents, detergents, and metal ions. Likewise, kinetic parameters for pNPP are: = 49.6 µM, = 57 s , and = 1.15 × 10 s ·M . LipC is also able to hydrolyze olive oil and degrade several polyester-type polymers such as poly(butylene succinate) (PBS), poly(butylene succinate)- -(butylene adipate) (PBSA), and poly(ε-caprolactone) (PCL). Moreover, LipC can catalyze the synthesis of different sugar fatty acid esters by transesterification using vinyl laurate as an acyl donor, demonstrating its interest in different biotechnological applications.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms242317071