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Research article2020Peer reviewedOpen access

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

Abstract

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.

Published in

Communications biology
2020, Volume: 3, number: 1, article number: 673Publisher: NATURE RESEARCH

      Sustainable Development Goals

      SDG9 Industry, innovation and infrastructure

      UKÄ Subject classification

      Biochemistry and Molecular Biology

      Publication identifier

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

      Permanent link to this page (URI)

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