A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris - Université de Lorraine Accéder directement au contenu
Article Dans Une Revue Communications Biology Année : 2020

A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris

Alexandre Olry
Jean Louis Hilbert

Résumé

The synthesis of 3,5-dicaffeoylquinic acid (3,5-DiCQA) has attracted the interest of many researchers for more than 30 years. Recently, enzymes belonging to the BAHD acyltransferase family were shown to mediate its synthesis, albeit with notably low efficiency. In this study, a new enzyme belonging to the GDSL lipase-like family was identified and proven to be able to transform chlorogenic acid (5-O-caffeoylquinic acid, 5-CQA, CGA) in 3,5-DiCQA with a conversion rate of more than 60%. The enzyme has been produced in different expression systems but has only been shown to be active when transiently synthesized in Nicotiana benthamiana or stably expressed in Pichia pastoris. The synthesis of the molecule could be performed in vitro but also by a bioconversion approach beginning from pure 5-CQA or from green coffee bean extract, thereby paving the road for producing it on an industrial scale.
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Origine : Publication financée par une institution

Dates et versions

hal-03011470 , version 1 (18-10-2023)
hal-03011470 , version 2 (01-02-2024)

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Sissi Miguel, Guillaume Legrand, Léonor Duriot, Marianne Delporte, Barbara Menin, et al.. A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris. Communications Biology, 2020, 3 (1), pp.1-13. ⟨10.1038/s42003-020-01387-1⟩. ⟨hal-03011470v2⟩
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