Your browser doesn't support javascript.
loading
Engineering carboxylic acid reductases and unspecific peroxygenases for flavor and fragrance biosynthesis.
Agosto-Maldonado, Alejandra; Guo, Jiantao; Niu, Wei.
Afiliación
  • Agosto-Maldonado A; Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States.
  • Guo J; Department of Chemistry, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States; The Nebraska Center for Integrated Biomolecular Communication (NCIBC), University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States.
  • Niu W; Department of Chemical & Biomolecular Engineering, University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States; The Nebraska Center for Integrated Biomolecular Communication (NCIBC), University of Nebraska-Lincoln, Lincoln, Nebraska 68588, United States. Electronic address: wniu2@unl.edu.
J Biotechnol ; 385: 1-12, 2024 Apr 10.
Article en En | MEDLINE | ID: mdl-38428504
ABSTRACT
Emerging consumer demand for safer, more sustainable flavors and fragrances has created new challenges for the industry. Enzymatic syntheses represent a promising green production route, but the broad application requires engineering advancements for expanded diversity, improved selectivity, and enhanced stability to be cost-competitive with current methods. This review discusses recent advances and future outlooks for enzyme engineering in this field. We focus on carboxylic acid reductases (CARs) and unspecific peroxygenases (UPOs) that enable selective productions of complex flavor and fragrance molecules. Both enzyme types consist of natural variants with attractive characteristics for biocatalytic applications. Applying protein engineering methods, including rational design and directed evolution in concert with computational modeling, present excellent examples for property improvements to unleash the full potential of enzymes in the biosynthesis of value-added chemicals.
Asunto(s)
Palabras clave

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Oxidorreductasas / Odorantes Idioma: En Revista: J Biotechnol Asunto de la revista: BIOTECNOLOGIA Año: 2024 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Oxidorreductasas / Odorantes Idioma: En Revista: J Biotechnol Asunto de la revista: BIOTECNOLOGIA Año: 2024 Tipo del documento: Article