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Forskningsartikel2020Vetenskapligt granskadÖppen tillgång

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

Miguel, Sissi; Legrand, Guillaume; Duriot, Leonor; Delporte, Marianne; Menin, Barbara; Michel, Cindy; Olry, Alexandre; Chataigne, Gabrielle; Salwinski, Aleksander; Bygdell, Joakim; Vercaigne, Dominique; Wingsle, Gunnar; Hilbert, Jean Louis; Bourgaud, Frederic; Hehn, Alain; Gagneul, David

Sammanfattning

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. Miguel et al. identify a new enzyme belonging to the GDSL lipase-like family that is involved in the final stage of transformation of 5-CQA into 3,5-diCQA. This enzyme is able to realize an efficient transformation by over 60%, making the transformation process a valuable technological tool that can be easily transferred on an industrial scale.

Publicerad i

Communications biology
2020, Volym: 3, nummer: 1, artikelnummer: 673
Utgivare: NATURE RESEARCH

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      Bygga motståndskraftig infrastruktur, verka för en inkluderande och hållbar industrialisering samt främja innovation

      UKÄ forskningsämne

      Biokemi och molekylärbiologi

      Publikationens identifierare

      DOI: https://doi.org/10.1038/s42003-020-01387-1

      Permanent länk till denna sida (URI)

      https://res.slu.se/id/publ/109985