Bioprospecting for Thermozymes and Characterization of a Novel Lipolytic Thermozyme Belonging to the SGNH/GDSL Family of Hydrolases

Autor: Juan-José Escuder-Rodríguez, María-Eugenia DeCastro, Almudena Saavedra-Bouza, María-Isabel González-Siso, Manuel Becerra
Jazyk: angličtina
Rok vydání: 2022
Předmět:
Zdroj: International Journal of Molecular Sciences; Volume 23; Issue 10; Pages: 5733
RUC. Repositorio da Universidade da Coruña
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ISSN: 1422-0067
DOI: 10.3390/ijms23105733
Popis: [Abstract] Functional screenings were conducted on two metagenomic libraries from hot springs in order to find novel thermozymes with potential biotechnological applications. These included enzymes acting on plant cell walls such as endoglucanases and exoglucanases, β-glucosidases, xylanases, and β-xylosidases, and broad application enzymes such as proteases and lipolytic hydrolases. Of all the enzymes found by this bioprospection, we selected a novel lipolytic enzyme for further characterization. The protein was found to belong to the SGNH/GDSL family of hydrolases. It was purified and its biochemical parameters determined. We found that the enzyme was most active at 60 °C and pH 9 using pNP-laurate as substrate and was highly thermostable. It also showed preference for short-chained substrates and activation with temperature and with certain detergents such as Tween 80. Proteins of this family of hydrolases are relevant for their broad substrate specificity, that coupled with this protein’s high temperature optima, broad pH range, and thermostability further highlights its biotechnological potential. This research received financial support from XUNTA DE GALICIA “Consolidación GRC” co-financed by FEDER [Grant Number ED431C 2020/08], and MINISTERIO DE CIENCIA, INNOVACIÓN Y UNIVERSIDADES (MICINN) [Grant Number RTI2018-099249-B-I00] Xunta de Galicia; ED431C 2020/08
Databáze: OpenAIRE
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