TY - JOUR
T1 - Lipase-catalyzed epoxy-acid addition and transesterification
T2 - from model molecule studies to network build-up
AU - Bakkali-Hassani, Camille
AU - Poutrel, Quentin-Arthur
AU - Langenbach, Jakob
AU - Chappuis, Sélène
AU - Blaker, Jonny J.
AU - Gresil, Matthieu
AU - Tournilhac, François
N1 - Funding Information:
This work was supported by European Union’s Horizon 2020 FET Open Project Self-Healing Soft Robotics [grant agreement no. 828818]. The authors gratefully acknowledge the financial support from the ANR through the MATVIT project (ANR-18-CE06-0026-01). Meito Ltd is thanked for provision of enzyme samples. We thank Sophie Norvez for scientific discussion and Lara Chaouat for her participation in enzymatic assays and kinetic experiments.
Publisher Copyright:
©
PY - 2021/10/7
Y1 - 2021/10/7
N2 - Commercially available lipase from Pseudomonas stutzeri (lipase TL) is investigated as a biocatalyst for the formation of an acid-epoxy chemical network. Molecular model reactions are performed by reacting 2-phenyl glycidyl ether and hexanoic acid in bulk, varying two parameters: temperature and water content. Characterizations of the formed products by 1H NMR spectroscopy and gas chromatography-mass spectrometry combined with enzymatic assays confirm that lipase TL is able to simultaneously promote acid-epoxy addition and transesterification reactions below 100 °C and solely the acid-epoxy addition after denaturation at T > 100 °C. A prototype bio-based chemical network with β-hydroxyester links was obtained using resorcinol diglycidyl ether and sebacic acid as monomers with lipase TL as catalyst. Differential scanning calorimetry, attenuated total reflection, and swelling analysis confirm gelation of the network.
AB - Commercially available lipase from Pseudomonas stutzeri (lipase TL) is investigated as a biocatalyst for the formation of an acid-epoxy chemical network. Molecular model reactions are performed by reacting 2-phenyl glycidyl ether and hexanoic acid in bulk, varying two parameters: temperature and water content. Characterizations of the formed products by 1H NMR spectroscopy and gas chromatography-mass spectrometry combined with enzymatic assays confirm that lipase TL is able to simultaneously promote acid-epoxy addition and transesterification reactions below 100 °C and solely the acid-epoxy addition after denaturation at T > 100 °C. A prototype bio-based chemical network with β-hydroxyester links was obtained using resorcinol diglycidyl ether and sebacic acid as monomers with lipase TL as catalyst. Differential scanning calorimetry, attenuated total reflection, and swelling analysis confirm gelation of the network.
UR - https://www.scopus.com/pages/publications/85117514212
U2 - 10.1021/acs.biomac.1c00820
DO - 10.1021/acs.biomac.1c00820
M3 - Article
C2 - 34618426
AN - SCOPUS:85117514212
SN - 1525-7797
VL - 22
SP - 4544
EP - 4551
JO - Biomacromolecules
JF - Biomacromolecules
IS - 11
ER -