A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris. Miguel, S., Legrand, G., Duriot, L., Delporte, M., Menin, B., Michel, C., Olry, A., Chataigné, G., Salwinski, A., Bygdell, J., Vercaigne, D., Wingsle, G., Hilbert, J. L., Bourgaud, F., Hehn, A., & Gagneul, D. Communications Biology, 3(1):673, December, 2020. ![A GDSL lipase-like from Ipomoea batatas catalyzes efficient production of 3,5-diCQA when expressed in Pichia pastoris [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{miguel_gdsl_2020,
title = {A {GDSL} lipase-like from {Ipomoea} batatas catalyzes efficient production of 3,5-{diCQA} when expressed in {Pichia} pastoris},
volume = {3},
issn = {2399-3642},
url = {http://www.nature.com/articles/s42003-020-01387-1},
doi = {10.1038/s42003-020-01387-1},
abstract = {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.},
language = {en},
number = {1},
urldate = {2021-06-07},
journal = {Communications Biology},
author = {Miguel, Sissi and Legrand, Guillaume and Duriot, Léonor and Delporte, Marianne and Menin, Barbara and Michel, Cindy and Olry, Alexandre and Chataigné, 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},
month = dec,
year = {2020},
pages = {673},
}
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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 . 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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-\n O\n -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\n Nicotiana benthamiana\n or stably expressed in\n Pichia pastoris\n . 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