Modificación del gen lipA codificante de la lipasa de Pseudomonas aeruginosa PSA01 dirigida a la alteración de su selectividad hacia ácidos grasos de diferente longitud de cadena
Lipase LipA from Pseudomonas aeruginosa is characterized by hydrolyzing a wide range of esterified fatty acids in triacylglycerols, from those with 4 carbons to those with 20 carbons. In this research, we sought to reduce the enzyme preference towards the hydrolysis of fatty acids of certain chain l...
- Autores:
- Tipo de recurso:
- Fecha de publicación:
- 2023
- Institución:
- Universidad de la Sabana
- Repositorio:
- Repositorio Universidad de la Sabana
- Idioma:
- spa
- OAI Identifier:
- oai:intellectum.unisabana.edu.co:10818/60285
- Acceso en línea:
- https://hdl.handle.net/10818/60285
- Palabra clave:
- Lipasa de Pseudomonas aeruginosa
LipA, error prone PCR
Mutagénesis al azar
- Rights
- License
- Attribution-NonCommercial-NoDerivatives 4.0 Internacional
| Summary: | Lipase LipA from Pseudomonas aeruginosa is characterized by hydrolyzing a wide range of esterified fatty acids in triacylglycerols, from those with 4 carbons to those with 20 carbons. In this research, we sought to reduce the enzyme preference towards the hydrolysis of fatty acids of certain chain length. Chemo selective lipases are interesting industrially because they favor the catalysis of fatty acids of specific chain lengths, with other similar ones in the same molecule, promoting their enrichment or selection and reducing additional purification steps. In LipA, the structures of the active site related to its low chemo preference are unknown, and their identification is a must. Thus, a random mutagenesis method with the epPCR technique was used to obtain mutants with differential selectivity for fatty acids. Culture conditions were established for the controlled and safe cytoplasmic expression of lipA together with the lif gene, encoding the foldase essential for its folding, in a construct not previously evaluated for its expression in E |
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