Purification and measurement of enzymatic activity and kinetic parameters for homoserine dehydrogenase as therapeutic target in Malassezia furfur

Malassezia genus is composed by 17 different yeast species. It is a common yeast in the skin microbiota and it is often a commensal fungi incapable to cause damage in the host. However, some species are related with cutaneous and systemic diseases. Previous studies reported some target enzymes to in...

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Autores:
Pérez Franco, Diana Carolina
Triana Sierra, Sergio Helí
Celis Ramírez, Adriana Marcela
Tipo de recurso:
Trabajo de grado de pregrado
Fecha de publicación:
2018
Institución:
Universidad de los Andes
Repositorio:
Séneca: repositorio Uniandes
Idioma:
eng
OAI Identifier:
oai:repositorio.uniandes.edu.co:1992/60876
Acceso en línea:
http://hdl.handle.net/1992/60876
Palabra clave:
Enzimas
Malassezia furfur
Rights
openAccess
License
http://creativecommons.org/licenses/by-nc-nd/4.0/
Description
Summary:Malassezia genus is composed by 17 different yeast species. It is a common yeast in the skin microbiota and it is often a commensal fungi incapable to cause damage in the host. However, some species are related with cutaneous and systemic diseases. Previous studies reported some target enzymes to inhibit the growth of Malassezia spp., one of those is homoserine dehydrogenase. For that reason, the present research sought to purify and quantify the enzymatic activity of homoserine dehydrogenase with the future aim to prove the inhibition of Malassezia furfur growth by the inhibition of the enzyme. To carry out the purification and measurement of enzymatic activity, E. coli with a specific his-tagged clone of homoserine dehydrogenase was sow in LB agar. The clone expression was induced by IPTG 2mM in the third hour of incubation and then the culture was purified using 2 different techniques: affinity chromatography and dynabeads...