Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Anne-Hélène Jan"'
Publikováno v:
ChemBioChem
ChemBioChem, Wiley-VCH Verlag, 2018, 19 (17), pp.1839-1844. ⟨10.1002/cbic.201800279⟩
ChemBioChem, Wiley-VCH Verlag, 2018, 19 (17), pp.1839-1844. ⟨10.1002/cbic.201800279⟩
Lipases/acyltransferases, such as CpLIP2 from Candida parapsilosis and CduLAc from Candida dubliniensis, catalyze acyl transfer preferentially over hydrolysis if a suitable nucleophile is present, even in a medium with a high thermodynamic activity o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2ace585c902029e57f7e211bc78bc57d
https://hal.archives-ouvertes.fr/hal-01918036
https://hal.archives-ouvertes.fr/hal-01918036
Publikováno v:
Lipid Modification by Enzymes and Engineered Microbes
Lipid Modification by Enzymes and Engineered Microbes, Academic Press, 2018, 9780128131671. ⟨10.1016/B978-0-12-813167-1.00003-7⟩
Lipid Modification by Enzymes and Engineered Microbes, Academic Press, 2018, 9780128131671. ⟨10.1016/B978-0-12-813167-1.00003-7⟩
Lipases/acyltransferases are a special group of lipases with highly enhanced affinity for other nucleophiles than water compared to classical lipases. In the presence of a suitable acceptor, they catalyze acyltransfer reactions (such as alcoholysis,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::991493b4081cf51d40fe960f1d425456
https://hal.archives-ouvertes.fr/hal-01918043
https://hal.archives-ouvertes.fr/hal-01918043
Autor:
Casimir C. Akoh, Uwe T. Bornscheuer, Stefan Bruder, Henrike Brundiek, Hanna Büchsenschütz, Xiao Chen, Fang Cong, Jasmina Damnjanović, Elisabeth I.P. Delbeke, Li Deng, Albert J. Dijkstra, Eric Dubreucq, Richard A. Gross, Jens Grüninger, Zheng Guo, Silke Hackenschmidt, Hans Christian Holm, Yugo Iwasaki, Anne-Hélène Jan, Johannes Kabisch, Shigenobu Kishino, Leslie Kleiner, Robert Kourist, Jingbo Li, Lei Li, Fanny Longin, Shekar Mekala, Eva J. Moldenhauer, Per Munk Nielsen, Jun Ogawa, Isabel Oroz-Guinea, Jin-Byung Park, Jacob Nedergaard Pedersen, Anna Schweiger, Sascha Siebenhaller, Chris V. Stevens, Maeva Subileau, Christoph Syldatk, Michiki Takeuchi, Inge N.A. Van Bogaert, Kevin M. Van Geem, Xuebing Xu, Young Joo Yeon, Katja Zorn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bd232b1a385bc9361e9fa6bdc4d916a9
https://doi.org/10.1016/b978-0-12-813167-1.00021-9
https://doi.org/10.1016/b978-0-12-813167-1.00021-9
Publikováno v:
Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2017, 1865 (9), pp.1105-1113. ⟨10.1016/j.bbapap.2017.06.004⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2017, 1865 (9), pp.1105-1113. ⟨10.1016/j.bbapap.2017.06.004⟩
Lipases/acyltransferases homologous to CpLIP2 from Candida parapsilosis belong to the α/β hydrolase superfamily as lipase A from Moesziomyces antarcticus (Candida antarctica), and constitute a consistent phylogenetic subgroup with at least 56% iden
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1877661361a65c8dd319c2f6f3d7eaa4
https://hal.archives-ouvertes.fr/hal-01605542
https://hal.archives-ouvertes.fr/hal-01605542
Publikováno v:
Catalysis Science & Technology
Catalysis Science & Technology, Royal Society of Chemistry, 2017, 7 (12), pp.2566-2578. ⟨10.1039/c6cy01805j⟩
Catalysis Science & Technology, Royal Society of Chemistry, 2017, 7 (12), pp.2566-2578. ⟨10.1039/c6cy01805j⟩
International audience; The necessity to develop more eco-friendly processes in oleochemistry has recently led to a renewed consideration of lipases exhibiting high acyltransferase activity in hydrated media. Yet, what precisely differentiates a "usu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fe50e9e5674e077ca56bc1d16f6f736d
https://hal.inrae.fr/hal-02620298
https://hal.inrae.fr/hal-02620298
Akademický článek
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Publikováno v:
Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2016, 1864 (2), pp.187-194. ⟨10.1016/j.bbapap.2015.11.006⟩
Biochimica et Biophysica Acta-Proteins and Proteomics 2 (1864), 187–194. (2016)
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2016, 1864 (2), pp.187-194. ⟨10.1016/j.bbapap.2015.11.006⟩
Biochimica et Biophysica Acta-Proteins and Proteomics 2 (1864), 187–194. (2016)
Performing transesterifications in aqueous media is becoming a priority challenge in lipid biotechnology in order to develop more eco-friendly and efficient biocatalytic processes in systems containing both polar and apolar substrates. In this contex
Autor:
Marina Perez-Gordo, Véronique Perrier, Eric Dubreucq, Maeva Subileau, Hervé Nozach, Anne-Hélène Jan
Publikováno v:
Biochimica et Biophysica Acta Proteins and Proteomics
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩
Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩
Biochimica et Biophysica Acta Proteins and Proteomics, Elsevier, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩
Biochimica et Biophysica Acta Proteins and Proteomics, 2015, 1854 (10), pp.1400-1411. ⟨10.1016/j.bbapap.2015.06.012⟩
Because lipids are hydrophobic, the development of efficient bioconversions in aqueous media free of organic solvents is particularly challenging for green oleochemistry. Within this aim, enzymes exhibiting various abilities to catalyze acyltransfer
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5e4bab851a2062da4f376ba21c4121e5
https://hal.archives-ouvertes.fr/hal-01269354
https://hal.archives-ouvertes.fr/hal-01269354