Bioprospecting for Thermozymes and Characterization of a Novel Lipolytic Thermozyme Belonging to the SGNH/GDSL Family of Hydrolases
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Bioprospecting for Thermozymes and Characterization of a Novel Lipolytic Thermozyme Belonging to the SGNH/GDSL Family of HydrolasesAutor(es)
Data
2022-05-20Cita bibliográfica
Escuder-Rodríguez, J.-J.; DeCastro, M.-E.; Saavedra-Bouza, A.; González-Siso, M.-I.; Becerra, M. Bioprospecting for Thermozymes and Characterization of a Novel Lipolytic Thermozyme Belonging to the SGNH/GDSL Family of Hydrolases. Int. J. Mol. Sci. 2022, 23, 5733. https://doi.org/10.3390/ijms23105733
Resumo
[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.
Palabras chave
Bioprospection
Metagenomes
Thermozymes
SGNH/GDSL
Hydrolases
Metagenomes
Thermozymes
SGNH/GDSL
Hydrolases
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Dereitos
Atribución 4.0 Internacional
ISSN
1422-0067