Miguel, Sissi and Legrand, Guillaume and Duriot, Léonor and Delporte, Marianne and Menin, Barbara and Michel, Cindy and Olry, Alexandre and Chataigne, Gabrielle and Salwinski, Aleksander and Bygdell, Joakim and Vercaigne, Dominique and Wingsle, Gunnar and Hilbert, Jean Louis and Bourgaud, Frédéric and Hehn, Alain and Gagneul, David
(2020).
A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris.
Communications biology. 3
, 673
[Journal article]
![]() |
PDF
1MB |
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.
Authors/Creators: | Miguel, Sissi and Legrand, Guillaume and Duriot, Léonor and Delporte, Marianne and Menin, Barbara and Michel, Cindy and Olry, Alexandre and Chataigne, Gabrielle and Salwinski, Aleksander and Bygdell, Joakim and Vercaigne, Dominique and Wingsle, Gunnar and Hilbert, Jean Louis and Bourgaud, Frédéric and Hehn, Alain and Gagneul, David | ||||||
---|---|---|---|---|---|---|---|
Title: | A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris | ||||||
Series Name/Journal: | Communications biology | ||||||
Year of publishing : | 2020 | ||||||
Volume: | 3 | ||||||
Article number: | 673 | ||||||
Number of Pages: | 13 | ||||||
Publisher: | NATURE RESEARCH | ||||||
ISSN: | 2399-3642 | ||||||
Language: | English | ||||||
Publication Type: | Journal article | ||||||
Article category: | Scientific peer reviewed | ||||||
Version: | Published version | ||||||
Copyright: | Creative Commons: Attribution 4.0 | ||||||
Full Text Status: | Public | ||||||
Subjects: | (A) Swedish standard research categories 2011 > 1 Natural sciences > 106 Biological Sciences (Medical to be 3 and Agricultural to be 4) > Biochemistry and Molecular Biology | ||||||
URN:NBN: | urn:nbn:se:slu:epsilon-p-109985 | ||||||
Permanent URL: | http://urn.kb.se/resolve?urn=urn:nbn:se:slu:epsilon-p-109985 | ||||||
Additional ID: |
| ||||||
ID Code: | 21279 | ||||||
Faculty: | S - Faculty of Forest Sciences | ||||||
Department: | (S) > Dept. of Forest Genetics and Plant Physiology | ||||||
Deposited By: | SLUpub Connector | ||||||
Deposited On: | 19 Jan 2021 14:03 | ||||||
Metadata Last Modified: | 19 Jan 2021 14:11 |
Repository Staff Only: item control page