Biochemical characterization of a novel ß-galactosidase from Lacticaseibacillus zeae and its application in synthesis of lacto-N-tetraose.
J Dairy Sci
; 106(10): 6623-6634, 2023 Oct.
Article
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| MEDLINE
| ID: mdl-37210349
ABSTRACT
Lacto-N-tetraose (LNT) is one of the most important components of human milk oligosaccharides, which has various beneficial health effects. ß-Galactosidase is an important enzyme used in dairy processing. The transglycosylation activity of ß-galactosidases offers an attractive approach for LNT synthesis. In this study, we reported for the ï¬rst time the biochemical characterization of a novel ß-galactosidase (LzBgal35A) from Lacticaseibacillus zeae. LzBgal35A belongs to glycoside hydrolases (GH) family 35 and shared the highest identity of 59.9% with other reported GH 35 members. The enzyme was expressed as soluble protein in Escherichia coli. The purified LzBgal35A displayed optimal activity at pH 4.5 and 55°C. It was stable within the pH range of 3.5 to 7.0 and up to 60°C. Moreover, LzBgal35A could catalyze the synthesis of LNT via transferring the galactose residue from o-nitrophenyl-ß-galactopyranoside to lacto-N-triose II. Under optimal conditions, the conversion rate of LNT reached 45.4% (6.4 g/L) within 2 h, which was by far the highest yield of LNT synthesized through a ß-galactosidase-mediated transglycosylation reaction. This study demonstrated that LzBgal35A has great potential application in LNT synthesis.
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Bases de datos:
MEDLINE
Asunto principal:
Oligosacáridos
/
Lacticaseibacillus
Límite:
Humans
Idioma:
En
Revista:
J Dairy Sci
Año:
2023
Tipo del documento:
Article