Modulation of the Biocatalytic Properties of a Novel Lipase from Psychrophilic <i>Serratia </i>sp. (USBA-GBX-513) by Different Immobilization Strategies

• Main Authors: Mónica Ruiz, Esteban Plata, John J. Castillo, Claudia C. Ortiz, Gina López, Sandra Baena, Rodrigo Torres, Roberto Fernandez-Lafuente
• Format: Article
• Language: English
• Published: MDPI AG 2021-03-01
• Series: Molecules
• Subjects: lipase from psychrophilic microorganism; immobilization; interfacial activation; hyperactivation; USBA-GBX-513
• Online Access: https://www.mdpi.com/1420-3049/26/6/1574

In this work, the effect of different immobilization procedures on the properties of a lipase obtained from the extremophilic microorganism <i>Serratia sp</i>. USBA-GBX-513, which was isolated from Paramo soils of Los Nevados National Natural Park (Colombia), is reported. Different Shepharose beads were used: octyl-(OC), octyl-glyoxyl-(OC-GLX), cyanogen bromide (BrCN)-, and Q-Sepharose. The performance of the different immobilized extremophile lipase from <i>Serratia</i> (ESL) was compared with that of the lipase B from <i>Candida antarctica</i> (CALB). In all immobilization tests, hyperactivation of ESL was observed. The highest hyperactivation (10.3) was obtained by immobilization on the OC support. Subsequently, the thermal stability at pH 5, 7, and 9 and the stability in the presence of 50% (<i>v</i>/<i>v</i>) acetonitrile, 50% dioxane, and 50% tetrahydrofuran solvents at pH 7 and 40 °C were evaluated. ESL immobilized on octyl-Sepharose was the most stable biocatalyst at 90 °C and pH 9, while the most stable preparation at pH 5 was ESL immobilized on OC-GLX-Sepharose supports. Finally, in the presence of 50% (<i>v</i>/<i>v</i>) tetrahydrofuran (THF) or dioxane at 40 °C, ESL immobilized on OC-Sepharose was the most stable biocatalyst, while the immobilized preparation of ESL on Q-Sepharose was the most stable one in 40% (<i>v</i>/<i>v</i>) acetonitrile<b>. </b>