Efficient monoacylglycerol synthesis by carboxylesterase EstGtA2 from Geobacillus thermodenitrificans in a solvent-free two-phase system.
Enzymatic monoacylglycerol synthesis
Lipolytic enzyme
Monoacylglycerol
Solvent-free two-phase system
Thermal-tolerant enzyme
Journal
Journal of bioscience and bioengineering
ISSN: 1347-4421
Titre abrégé: J Biosci Bioeng
Pays: Japan
ID NLM: 100888800
Informations de publication
Date de publication:
Aug 2022
Aug 2022
Historique:
received:
24
12
2021
revised:
25
03
2022
accepted:
05
05
2022
pubmed:
2
6
2022
medline:
5
8
2022
entrez:
1
6
2022
Statut:
ppublish
Résumé
The present study investigated high-yield monoacylglycerol (MAG) synthesis by bacterial lipolytic enzymes in a solvent-free two-phase system. Esterification by monoacylglycerol lipase from Bacillus sp. H-257 (H257) required a high glycerol/fatty acid molar ratio for efficient MAG synthesis. Screening of H257 homologues revealed that carboxylesterase derived from Geobacillus thermodenitrificans, EstGtA2, exhibited a higher esterification rate than H257. Moreover, neutralizing the pH of the acidic reaction solution by adding potassium hydroxide (KOH) solution further increased the esterification rate. The esterification rate by EstGtA2 reached 75% under conditions of equivalent molar amounts of glycerol and fatty acid, and the MAG rate (MAG/total glyceride) was 97%. The neutralized pH of the reaction solution likely affected the thermal stability of EstGtA2 during the esterification reaction. Screening for thermal-tolerant variants revealed that the EstGtA2
Identifiants
pubmed: 35644798
pii: S1389-1723(22)00128-1
doi: 10.1016/j.jbiosc.2022.05.004
pii:
doi:
Substances chimiques
Enzymes, Immobilized
0
Fatty Acids
0
Monoglycerides
0
Solvents
0
Carboxylesterase
EC 3.1.1.1
Glycerol
PDC6A3C0OX
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
89-94Informations de copyright
Copyright © 2022 The Society for Biotechnology, Japan. Published by Elsevier B.V. All rights reserved.