Caracterización biofísica y estructural de la subunidad biotin-carboxilasa de la enzima acetil-coa carboxilasa de una microalga oleaginosa ankistrodesmus SP
The depletion of fossil resources, concerns about their emissions and, above all, the increase in environmental pollution have led to the search for new sources of renewable energy based on natural raw materials such as oleaginous microalgae. Among these, Ankistrodesmus sp., a microalga native to th...
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| Formato: | tesis de maestría |
| Fecha de publicación: | 2024 |
| País: | Perú |
| Recursos: | Universidad Nacional De La Amazonía Peruana |
| Repositorio: | UNAPIquitos-Institucional |
| Idioma: | español |
| OAI Identifier: | oai:repositorio.unapiquitos.edu.pe:20.500.12737/10888 |
| Acesso em linha: | https://hdl.handle.net/20.500.12737/10888 |
| Access Level: | acceso abierto |
| Palavra-chave: | Biotina Propiedades fisicoquímicas Enzimad Microalgas Oleaginosa ankistrodesmus https://purl.org/pe-repo/ocde/ford#2.04.01 |
| Resumo: | The depletion of fossil resources, concerns about their emissions and, above all, the increase in environmental pollution have led to the search for new sources of renewable energy based on natural raw materials such as oleaginous microalgae. Among these, Ankistrodesmus sp., a microalga native to the Peruvian Amazon, can be used for bioenergy purposes. The aim of the present work was the biophysical and structural characterization of the biotin carboxylase subunit of the ACCase enzyme from an Amazonian oleaginous microalga, Ankistrodesmus sp. The gene encoding BC was cloned, expressed and the recombinant protein (AnkBC) purified by chromatography. Subsequently, AnkBC was characterized biophysically and structurally. The purified monomeric AnkBC protein had a molecular mass of 56 kDa on SDS PAGE. Multi-angle light scattering profiling (SEC-MALS) showed that the protein forms a homodimer of 105,47 kDa. Circular dichroism spectroscopy revealed that the homodimer is conformationally stable. Finally, in silico analysis of AnkBC revealed a three-domain homodimer characteristic of the ATP-dependent biotin-binding superfamily. In conclusion, the study provides a detailed understanding of the biophysical and structural properties of the biotin carboxylase (BC) subunit from Ankistrodesmus sp. From its cloning to the determination of its three-dimensional structure by bioinformatics methods, this information not only deepens the fundamental knowledge about the ACCase enzyme in oleaginous microalgae, but also opens new possibilities in the practical application of this information in biotechnology and biofuel production. |
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