Transesterification with CE15 glucuronoyl esterase from Cerrena unicolor reveals substrate preferences.
Biotechnol Lett
; 46(1): 107-114, 2024 Feb.
Article
em En
| MEDLINE
| ID: mdl-38150097
ABSTRACT
PURPOSE:
Glucuronoyl esterases (GE, family CE15) catalyse the cleavage of ester linkages in lignin-carbohydrate complexes (LCCs), and this study demonstrate how transesterification reactions with a fungal GE from Cerrena unicolor (CuGE) can reveal the enzyme's preference for the alcohol-part of the ester-bond.METHODS:
This alcohol-preference relates to where the ester-LCCs are located on the lignin molecule, and has consequences for how the enzymes potentially interact with lignin. It is unknown exactly what the enzymes prefer; either the α-benzyl or the γ-benzyl position. By providing the enzyme with a donor substrate (the methyl ester of either glucuronate or 4-O-methyl-glucuronate) and either one of two acceptor molecules (benzyl alcohol or 3-phenyl-1-propanol) we demonstrate that the enzyme can perform transesterification and it serves as a method for assessing the enzyme's alcohol preferences.CONCLUSION:
CuGE preferentially forms the γ-ester from the methyl ester of 4-O-methyl-glucuronate and 3-phenyl-1-propanol and the enzyme's substrate preferences are primarily dictated by the presence of the 4-O-methylation on the glucuronoyl donor, and secondly on the type of alcohol.Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Propanóis
/
Polyporales
/
Esterases
/
Lignina
Idioma:
En
Revista:
Biotechnol Lett
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
Dinamarca
País de publicação:
Holanda