Inhibition of lytic polysaccharide monooxygenase by natural plant extracts
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Inhibition of lytic polysaccharide monooxygenase by natural plant extracts. / Tokin, Radina; Frandsen, Kristian E. H.; Ipsen, Johan Ørskov; Lo Leggio, Leila; Poojary, Mahesha M.; Berrin, Jean-Guy; Grisel, Sacha; Brander, Søren; Jensen, Poul Erik; Johansen, Katja Salomon.
In: New Phytologist, Vol. 232, No. 3, 2021, p. 1337–1349.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Inhibition of lytic polysaccharide monooxygenase by natural plant extracts
AU - Tokin, Radina
AU - Frandsen, Kristian E. H.
AU - Ipsen, Johan Ørskov
AU - Lo Leggio, Leila
AU - Poojary, Mahesha M.
AU - Berrin, Jean-Guy
AU - Grisel, Sacha
AU - Brander, Søren
AU - Jensen, Poul Erik
AU - Johansen, Katja Salomon
PY - 2021
Y1 - 2021
N2 - Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported.In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC–MS, we successfully identified a natural LPMO inhibitor.Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC–MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1.The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts.
AB - Lytic polysaccharide monooxygenases (LPMOs) are monocopper enzymes of industrial and biological importance. In particular, LPMOs play important roles in fungal lifestyle. No inhibitors of LPMOs have yet been reported.In this study, a diverse library of 100 plant extracts was screened for LPMO activity-modulating effects. By employing protein crystallography and LC–MS, we successfully identified a natural LPMO inhibitor.Extract screening revealed a significant LPMO inhibition by methanolic extract of Cinnamomum cassia (cinnamon), which inhibited LsAA9A LPMO from Lentinus similis in a concentration-dependent manner. With a notable exception, other microbial LPMOs from families AA9 and AA10 were also inhibited by this cinnamon extract. The polyphenol cinnamtannin B1 was identified as the inhibitory component by crystallography. Cinnamtannin B1 was bound to the surface of LsAA9A at two distinct binding sites: one close to the active site and another at a pocket on the opposite side of the protein. Independent characterization of cinnamon extract by LC–MS and subsequent activity measurements confirmed that the compound inhibiting LsAA9A was cinnamtannin B1.The results of this study show that specific natural LPMO inhibitors of plant origin exist in nature, providing the opportunity for future exploitation of such compounds within various biotechnological contexts.
KW - Cinnamomum cassia
KW - cinnamtannin B1
KW - inhibitor
KW - Lentinus similis
KW - LPMO
KW - lytic polysaccharide monooxygenase
KW - plant extract
U2 - 10.1111/nph.17676
DO - 10.1111/nph.17676
M3 - Journal article
C2 - 34389999
VL - 232
SP - 1337
EP - 1349
JO - New Phytologist
JF - New Phytologist
SN - 0028-646X
IS - 3
ER -
ID: 276232301