Biochemical identification of D-mannose 2-epimerase from Cytophagaceae bacterium SJW1-29 for efficient bioconversion of D-glucose to D-mannose.
Enzyme Microb Technol
; 179: 110465, 2024 Sep.
Article
em En
| MEDLINE
| ID: mdl-38852283
ABSTRACT
Enzymatic production of D-mannose attracts increasing attention because of the health effects and commercial values of D-mannose. Several kinds of epimerases or isomerases have been used for enzymatic production of D-mannose from D-glucose or D-fructose. D-Mannose epimerase (MEase), belonging to N-acyl-D-glucosamine 2-epimerase superfamily enzymes, catalyzes the C-2 epimerization between D-glucose and D-mannose. In this study, a novel MEase was identified from Cytophagaceae bacterium SJW1-29. Sequence and structure alignments indicate that it is highly conserved with the reported R. slithyformis MEase with the known crystal structure. It was a metal-independent enzyme, with an optimal pH of 8.0 and an optimal temperature of 40⯰C. The specific activities on D-glucose and D-mannose were 2.90 and 2.96â¯U/mg, respectively. The Km, kcat, and kcat/Km on D-glucose were measured to be 194.9â¯mM, 2.72â¯s-1, and 0.014â¯mM-1 s-1, respectively. The purified enzyme produced 23.15â¯g/L of D-mannose from 100â¯g/L of D-glucose at pH 8.0 and 40 °C for 8â¯h, with a conversion rate of 23.15â¯%.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Carboidratos Epimerases
/
Glucose
/
Manose
Idioma:
En
Revista:
Enzyme Microb Technol
Ano de publicação:
2024
Tipo de documento:
Article
País de afiliação:
China