May 1, 2024Journal of Agricultural and Food ChemistryOpen Access

Improved Enzymatic Production of the Fucosylated Human Milk Oligosaccharide LNFP II with GH29B α-1,3/4-l-Fucosidases

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YYYa-Ya YangJiangsu University ATAlbert Thor ThorhallssonJiangsu University CRCarme RoviraInstitució Catalana de Recerca i Estudis Avançats

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Implication

Biochemical analysis demonstrates efficient synthesis of lacto-N-fucopentaose II in recombinant enzyme assays, suggesting scalable manufacturing of infant formula ingredients.

Key Points

Record transglycosylation yields of the human milk oligosaccharide lacto-N-fucopentaose II were achieved using wild-type GH29B alpha-l-fucosidases, overcoming common hydrolytic limits.
Transglycosylation yields reached 91% for SpGH29C and 65% for CpAfc2 enzymes, representing the highest transfucosylation efficiencies reported to date for lacto-N-tetraose conversion.
Molecular dynamics simulations and enzymatic assays characterized five GH29B alpha-l-fucosidases, revealing how loop mutations modulate transfucosylation and secondary hydrolysis.
May enable efficient industrial manufacturing of lacto-N-fucopentaose II as a novel infant formula ingredient, while establishing engineering targets to suppress secondary hydrolysis.

Cite This Study

Yang et al. (2024) studied this question.

synapsesocial.com/papers/68e6c033b6db64358763f783 https://doi.org/10.1021/acs.jafc.4c01547

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Implication

Biochemical analysis demonstrates efficient synthesis of lacto-N-fucopentaose II in recombinant enzyme assays, suggesting scalable manufacturing of infant formula ingredients.

Improved Enzymatic Production of the Fucosylated Human Milk Oligosaccharide LNFP II with GH29B α-1,3/4-l-Fucosidases

Discussion

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Implication

Key Points

Cite This Study

Improved Enzymatic Production of the Fucosylated Human Milk Oligosaccharide LNFP II with GH29B α-1,3/4-l-Fucosidases

Discussion

Member takes

Implication

Key Points

Cite This Study

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