{"id":4396,"date":"2014-12-03T11:49:14","date_gmt":"2014-12-03T11:49:14","guid":{"rendered":"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=4396"},"modified":"2025-10-10T07:33:39","modified_gmt":"2025-10-10T07:33:39","slug":"jean-michel-girardet-2","status":"publish","type":"page","link":"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=4396","title":{"rendered":"Jean-Michel Girardet"},"content":{"rendered":"<p><strong><em><a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/wp-content\/uploads\/2016\/09\/Girardet-JM.1024.jpg\"><img loading=\"lazy\" decoding=\"async\" class=\"wp-image-7034 alignleft\" src=\"https:\/\/mycor.iam.inrae.fr\/IAM\/wp-content\/uploads\/2016\/09\/Girardet-JM.1024-225x300.jpg\" alt=\"\" width=\"150\" height=\"195\" \/><\/a><span style=\"color: #800080\">PAST AND CURRENT FUNCTIONS:<\/span><\/em><\/strong><\/p>\n<p>\u2013 2015: Currently assigned to UMR 1136 INRAE\/University of Lorraine <strong>IAM<\/strong> as Research Engineer. Manager of the &#8216;Structural and Functional Approaches of Cellular InterActions&#8217; (ASIA) platform located at the Faculty of Sciences and Technologies: <a href=\"https:\/\/a2f.univ-lorraine.fr\/asia\/\"><strong>https:\/\/a2f.univ-lorraine.fr\/asia\/<\/strong><\/a><\/p>\n<p>\u2013 1993-2014: Research Engineer in Food Biochemistry assigned to UR AFPA (currently known as <strong>L2A<\/strong>), USC INRAE 340, University of Lorraine, France.<\/p>\n<p><span style=\"color: #800080\"><strong><em>QUALIFICATIONS:<\/em><\/strong><\/span><\/p>\n<p>\u2013 2012:\u00a0<strong>H.D.R.<\/strong>\u00a0(Qualified Research Supervisor) from the University of Lorraine, France:\u00a0<em>\u2018Technofunctional and Biofunctional Properties of Milk Proteins and Peptides\u2019.<\/em><\/p>\n<p>\u2013 1992:\u00a0<strong>Ph.D.<\/strong>\u00a0in Applied Biochemistry from the University of Nancy 1, France\u00a0: \u2018<em>Component PP3 of Milk: Preparation, Origin, Study of its Glycan Moiety, Role in the Inhibition of Lipolysis<\/em>\u2019. (INRAE-Region of Lorraine scholarship)<\/p>\n<p>&nbsp;<\/p>\n<p><em>\u00a0<span style=\"color: #800080\"><strong>PEER-REVIEWED PUBLICATIONS 2022-2026:<\/strong><\/span><\/em><\/p>\n<p><strong>2025<\/strong><\/p>\n<p>Laroussi H., Maffo-Woulefack R., Cappele J., Alaoui H.S., Lessure L., Zahaf M., <strong>Girardet J.M.<\/strong>, Cl\u00e9ment E., Thiriet L., Bertin S., Begue D., Douzi B., Roussel Y., Didierjean C., Favier F., Tsan P., Leblond-Bourget N. &amp; Nicolas Soler N. (2025). Two OB-fold proteins from a Gram-positive conjugative element engage in relaxosome assembly and DNA processing. <em>Nucleic Acids Research, in press<\/em><\/p>\n<p>Cama\u00f1o Echavarr\u00eda J.A., Math\u00e9 C., <strong>Girardet J.M.<\/strong>, Paris C, Udenigwe C.C., Selmeczi K, &amp; Canabady-Rochelle L. (2025). Identification of Ni2+-binding peptides in sunflower meal protein hydrolysate for deeper understanding of peptide-metal interactions. <em>Journal of Inorganic Biochemistry, 269<\/em>, 112877. <strong><span style=\"color: #3366ff\">https:\/\/doi.org\/10.1016\/j.jinorgbio.2025.112877<\/span><\/strong><\/p>\n<p>Cama\u00f1o Echavarr\u00eda J.A., Irankunda R., Arnoux P., Math\u00e9 C., <strong>Girardet J.M.<\/strong>, Cakir-Kiefer C., Risler A., Stefan L., Paris C., Zapata Montoya J.E., Selmeczi K., &amp; Canabady-Rochelle L. (2025). Characterization and Bioactivities of Gelatin Hydrolysates of Red Tilapia (<em>Oreochromis<\/em> spp.) Scale By-products. <em>ACS Food Science &amp; Technology<\/em>,<em> 5<\/em>, 1100-1115. <strong><span style=\"color: #3366ff\">https:\/\/doi.org\/10.1021\/acsfoodscitech.4c00918<\/span><\/strong><\/p>\n<p>Irankunda R., Cama\u00f1o Echavarr\u00eda J.A., El Hajj S., Paris C., Cakir-Kiefer C., <strong>Girardet J.M.<\/strong>, Arnoux P., Muhr L., Canabady-Rochelle L. (2025). <em>Pisum Sativum<\/em> Protein Hydrolysates: Production, Sensitive Screening of Nickel Chelating Peptides and Evaluation of Antioxidant Properties. <em>Food Bioscience<\/em>, 106001. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-05004501v1<\/span><\/strong><\/p>\n<p><strong>2024<\/strong><\/p>\n<p>Baratzhanova G., <strong>Girardet J.M.<\/strong>, Fournier A., Djansugurov, L., &amp; Cakir-Kiefer C. (2024). Application of the switchSENSE\u00ae technology for real-time study of pesticides interaction with biological molecules. <em>BIO Web of Conferences, 100<\/em>, 03003. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-05005153v1<\/span><\/strong><\/p>\n<p>Bj\u00f8rlie M., Irankunda R., Yesiltas B., Moltke S\u00f8rensen A.D., <strong>Girardet J.M.<\/strong>, Boschi-M\u00fcller S., Jacobsen C., &amp; Canabady-Rochelle L. (2024). Metal-chelating antioxidant peptides &#8211; Biosensor screening methods as alternatives to the ferrozine assay. <em>Journal of the American Oil Chemists&#8217; Society<\/em>,<em>101<\/em>, 827-837. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04700891v1<\/span><\/strong><\/p>\n<p><strong>2023<\/strong><\/p>\n<p>Safran J., Tabi W., Ung V., Lemaire A., Habrylo O., Bouckaert J., Rouffle M., Voxeur A., Pongrac P., Bassard S., Molini\u00e9 R., Fontaine J.-X., Pilard S., Pau-Roblot C., Bonnin E., Larsen D.S., Morel-Rouhier M., <strong>Girardet J.M.<\/strong>, Lefebvre V., S\u00e9n\u00e9chal F., Mercadante D., &amp; Pelloux J. (2023). Differences in the crystal structure of plant polygalacturonases specify enzymes&#8217; dynamics and processivities to fine-tune cell wall pectins. <em>The Plant Cell, 35, <\/em>3073-3091<em>. <\/em><strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-03764722v1<\/span><\/strong><\/p>\n<p><span style=\"color: #000000\"><strong>2022<\/strong><\/span><\/p>\n<p>Narmuratova Z., Hentati F., <strong>Girardet J.M.<\/strong>, Narmuratova M., &amp; Cakir-Kiefer C. (2022). Equine lactoferrin: Antioxidant properties related to divalent metal chelation<em>. LWT Food Science and Technology, 161<\/em>, 113426.<span style=\"color: #3366ff\"><strong>\u00a0https:\/\/hal.univ-lorraine.fr\/hal-04006980v1<\/strong><\/span><\/p>\n<p><span style=\"color: #800080\"><em><strong>COMMUNICATIONS 2022-2027:<\/strong><\/em><\/span><\/p>\n<p>Tsan P., Cappele J., Laroussi H., Cl\u00e9ment E., Begue D., Maffo-Woulefack R., <strong>Girardet J.M.<\/strong>, Leblond-Bourget N., Soler N., Didierjean C., Favier F. NMR solution structure of OrfM from ICESt3 of <em>Streptococcus thermophilus<\/em>. International Conference on type IV secretion system (T4SS), February 17 \u2013 20, 2025, Nancy, France.<\/p>\n<p>Baubekova A., Hentati, F., Akindykova A., Jurjanz S., <strong>Girardet J.M.<\/strong>, Cakir C. Complexation of copper(II) ion by camel milk casein tryptic hydrolysate. International Conference on Food Chemistry &amp; Technology (FCT 2024), November 25 \u2013 27, 2024, Valencia, Spain.<\/p>\n<p>Cama\u00f1o Echavarr\u00eda J.A., Irankunda R., Arnoux P., <strong>Girardet J.M.<\/strong>, Math\u00e9,C., Stefan,L. Selmeczi,K., Canabady-Rochelle L. Screening of Metal-Chelating Peptides in Protein Hydrolysates from Agro-industrial by-products using switchSENSE\u00ae Technology. 2nd International conference on Metal-Binding Peptides: Methodologies and Applications, Toulouse, France. July 10 \u2013 12, 2024.<\/p>\n<p>Gaviria Gaviria, Y.S., Cama\u00f1o Echavarr\u00eda J.A., Arnoux P., <strong>Girardet J.M.<\/strong>, Paris C., Math\u00e9 C., Zapata Montoya J.E., Canabady-Rochelle L. Metal complexation abilities of protein hydrolysates from the Californian red worm. Process Development Symposium Europe, June 26 \u2013 28, 2024, Nancy, France. <span style=\"color: #3366ff\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-04762981v1<\/strong><\/span><\/p>\n<p>Baratzhanova G., <strong>Girardet J.M.<\/strong>, Fournier A., Djansugurova L., Cakir-Kiefer C. Application of the switchSENSE\u00ae technology for real-time study of pesticides interaction with biological molecules. International Forum Modern Trends in Sustainable Development of Biological Sciences, Al-Farabi Kazakh National University, Almaty, Kazakhstan, March 27 \u2013 28, 2024.<\/p>\n<p><strong>Girardet J.M.<\/strong> Investigation of non-enzymatic deamidation of equine and camel milk proteins at their Asn-Gly sequences. Janeiro-na-Madeira (JnM-2024) Winter-Summer Event, Deamidation and Isoaspartate session, Funchal, Madeira, Portugal, January 8 \u2013 12, 2024. <strong><span style=\"color: #3366ff\"><em>Oral communication<\/em><\/span>.<\/strong><\/p>\n<p>Cama\u00f1o Echavarr\u00eda J.A., Irankunda R., Arnoux P., <strong>Girardet J.M.<\/strong>, Risler A., Zapata J.E., Stefan L., Selmeczi K., Canabady-Rochelle L. Production of Metal-Chelating Peptide Hydrolysates from Gelatin Protein Extracted from Red Tilapia (<em>Oreochromis<\/em> spp.) Scales and Evaluation of their bioactivities. International Symposium on Bioactive Peptides, Niagara Falls, ON, Canada, September 27 \u2013 29,2023. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04258181v1<\/span><\/strong><\/p>\n<p>Irankunda R., Cama\u00f1o Echavarr\u00eda J.A., Bounaceur R., El Hajj S., Paris C., Selmeczi K., <strong>Girardet J.M<\/strong>., Boshi-Muller S., Muhr L., Canabady-Rochelle L. <em>In silico<\/em> enzymatic production of metal-chelating peptides from pea proteins and simulation of their separation in IMAC. International Symposium on Bioactive Peptides, Niagara Falls, ON, Canada, September 27 \u2013 29,2023. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04258193v1<\/span><\/strong><\/p>\n<p>Irankunda R., Cama\u00f1o Echavarr\u00eda J.A., Paris C., Pontvianne S., Stefan L., Selmeczi K., <strong>Girardet J.M.<\/strong>, Boschi-Muller S., Muhr L., &amp; Canabady-Rochelle L. Deciphering Peptide-Metal ion Complexation for Simulating Peptides Separation in IMAC. 23<sup>rd<\/sup> GFPP Meeting on Peptides and Proteins, Fournols, France, September 17 \u2013 21, 2023.<\/p>\n<p>Bj\u00f8rlie M., Irankunda R., Canabady-Rochelle L., <strong>Girardet J.M.<\/strong>, Boschi-M\u00fcller S., Yesiltas B., Moltke S\u00f8rensen A.D., &amp; Jacobsen C. Screening of metal-chelating peptides and hydrolysates using Surface Plasmon Resonance and switchSENSE. AOCS conference: Effect of chelating-peptides and pea protein hydrolysates on lipid oxidation, Denver, CO, USA, April 30 &#8211; May 3, 2023. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04258864v1<\/span><\/strong><\/p>\n<p>El Hajj S., Irankunda R., Cama\u00f1o Echavarr\u00eda J.A., <strong>Girardet J.M.<\/strong>, Boschi-Muller S., Gaucher C., &amp; Canabady-Rochelle L. Methodologies for Screening Metal-Chelating Peptides in Protein Hydrolysates for their Antioxidant Properties. International Conference on Metal-Binding peptides MBP 2022. Nancy, France, July 05 \u2013 08, 2022. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04259077v1<\/span><\/strong><\/p>\n<p>Bj\u00f8rlie M., Irankunda R., <strong>Girardet J.M.<\/strong>, Boschi-Muller S., Yesiltas B., Moltke S\u2000Rensen A.D., Jacobsen C, Canabady-Rochelle L. Screening of metal-chelating peptides using surface plasmon resonance and switchSENSE. AOAC conference, Scottdale, AZ, USA, August 26<sup>th<\/sup> \u2013 September 1<sup>st<\/sup>, 2022.<\/p>\n<p>Irankunda R., Cama\u00f1o Echavarr\u00eda J.A., Paris C., Pontvianne S., Stefan L., Selmeczi K., <strong>Girardet J.M.<\/strong>, Boschi-Muller S., Muhr L., &amp; Canabady-Rochelle L. Metal-Chelating Peptides Separation: from SPR affinity constant determination up to their IMAC simulation. International Conference on Metal-Binding peptides MBP 2022. Nancy, France, July 05 \u2013 08, 2022. <strong><span style=\"color: #3366ff\">https:\/\/hal.univ-lorraine.fr\/hal-04259072v1<\/span><\/strong><\/p>\n<p>Hentati F., Selmeczi K., Akindykova A., Jurjanz S., <strong>Girardet J.M.<\/strong>, Baubekova A., &amp; Cakir-Kiefer C. Complexation of copper(II) ion by camel milk casein tryptic hydrolysate. International Conference on Metal-Binding peptides MBP 2022. Nancy, France, July 05 \u2013 08, 2022.<\/p>\n<p>Cakir-Kiefer C., Hentati F., Narmuratova Z., <strong>Girardet J.M.<\/strong>, &amp; Narmuratova M. Equine lactoferrin: antioxidant properties related to divalent metal chelation. International Conference on Metal-Binding peptides MBP 2022. Nancy, France, July 05 \u2013 08, 2022. <span style=\"color: #3366ff\"><em>Invited lecture.<\/em><\/span><\/p>\n<p><span style=\"color: #800080\"><em><strong>PEER-REVIEWED PUBLICATIONS 2016-2021:<\/strong><\/em><\/span><\/p>\n<p><span style=\"color: #000000\"><strong>2021<\/strong><\/span><\/p>\n<p>El Hajj S., Sep\u00falveda-Rinconi T., <strong>Girardet J.M.<\/strong>, Cakir-Kiefer C., Stefan L., Zapata-Montoya J.E., Boshi-Muller S., Gaucher C. &amp; Canabady-Rochelle L. (2021) Electrically switchable nanolever technology for the screening of metal-chelating peptides in hydrolysates. <em>Journal of Agricultural and Food Chemistry<\/em>, <em>69<\/em>, 8819-8827. <strong><a class=\"ref-halid\" title=\"\" href=\"https:\/\/hal.univ-lorraine.fr\/hal-03447722v1\" data-toggle=\"tooltip\" data-placement=\"bottom\" data-original-title=\"Voir la ressource\">https:\/\/hal.univ-lorraine.fr\/hal-03447722<small>v1<\/small><\/a><\/strong><\/p>\n<p>Perrot T., Schwartz M., Deroy A., <strong>Girardet J.M.<\/strong>, Kohler A., Morel-Rouhier M., Favier F., Gelhaye E. &amp; Didierjean C. (2021). Diversity of Omega Glutathione Transferases in mushroom-forming fungi revealed by phylogenetic, transcriptomic, biochemical and structural approaches. <em>Fungal Genetics and Biology, 148<\/em>, 103506. <strong><a class=\"doi\" title=\"Persistent link using digital object identifier\" href=\"https:\/\/hal.univ-lorraine.fr\/\" target=\"_blank\" rel=\"noreferrer noopener\" aria-label=\"Persistent link using digital object identifier\">https:\/\/hal.univ-lorraine.fr\/<\/a><a class=\"ref-halid\" title=\"\" href=\"https:\/\/hal.univ-lorraine.fr\/hal-03143927v1\" data-toggle=\"tooltip\" data-placement=\"bottom\" data-original-title=\"Voir la ressource\">hal-03143927<small>v1<\/small><\/a><\/strong><\/p>\n<p>Bchini R., <strong>Girardet J.M.<\/strong>, Sormani R., Gelhaye E. &amp; Morel-Rouhier M. (2021). Oxidized glutathione promotes association between Eukaryotic Translation Elongation Factor 1B\u03b3 and Ure2p glutathione transferase from Phanerochaete chrysosporium. The FEBS Journal, 288, 2956-2969. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-03143938v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-03143938v1<\/strong><\/a><\/p>\n<p>El Hajj S., Sep\u00falveda-Rinconi T., Selmeczi K., Paris C., Giraud T., Csire G., Stefan L., <strong>Girardet J.M.<\/strong>, Desobry S., Bouhallab S., Muhr L., Gaucher C. &amp; Canabady-Rochelle L. (2021) Chapter 19, Applications in Nutrition: Mineral-Binding. <em>In Biologically Active Peptides 1<sup>st<\/sup> Ed.: From basic science to applications for human health (Fidel Toldr\u00e1 and Jianping Wu, Eds.), pp 455-494<\/em>, <em>Elsevier. Academic Press<\/em> (512 pages).<br \/>\n<strong><a href=\"https:\/\/hal.univ-lorraine.fr\/\">https:\/\/hal.univ-lorraine.fr\/hal-03267562v1 \u00a0 \u00a0 \u00a0 \u00a0<\/a><a href=\"https:\/\/www.elsevier.com\/books\/biologically-active-peptides\/toldra\/978-0-12-821389-6\">ISBN 9780128213896<\/a><a href=\"https:\/\/hal.univ-lorraine.fr\/\">.<\/a><\/strong><\/p>\n<p><strong>2020<\/strong><\/p>\n<p>Roret, T., Alloing G., <strong>Girardet, J.M.<\/strong>, Perrot T., Dhalleine, T., Couturier J., Frendo P., Didierjean C. &amp; Rouhier N. (2020). <em>Sinorhizobium meliloti<\/em> YrbA binds divalent metal cations using two conserved histidines. <em>Bioscience Reports<\/em>, <em>40<\/em>, BSR20202956. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-03000204v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-03000204v1<\/strong><\/a><\/p>\n<p>Delannoy M., <strong>Girardet J.M.<\/strong>, Djelti F., Yen F.T. &amp; Cakir-Kiefer C. (2020). Affinity of chlordecone and chlordecol for human serum lipoproteins. <em>Environmental Toxicology and Pharmacology<\/em>, <em>80<\/em>, 103486. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02925906v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02925906v1<\/strong><\/a><\/p>\n<p>Vicente C.M., <strong>Girardet J.M.<\/strong>, H\u00f4tel L. &amp; Aigle B. (2020). Molecular dynamics to elucidate the DNA-binding activity of AlpZ, a member of the gamma-butyrolactone receptor family in <em>S. ambofaciens<\/em>. <em>Frontiers in Microbiology: Antimicrobials, Resistance and Chemotherapy<\/em>, <em>11<\/em>, 1255. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02935390v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02935390v1<\/strong><\/a><\/p>\n<p>Sylvestre-Gonon E., Schwartz M., <strong>Girardet J.M.<\/strong>, Hecker A. &amp; Rouhier N. (2020). Is there a role for tau glutathione transferases in tetrapyrrole metabolism and retrograde signalling in plants? <em>Philosophical Transactions of the Royal Society B,<\/em> <em>375<\/em>, 20190404. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02890959v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02890959v1<\/strong><\/a><\/p>\n<p><strong>2019<\/strong><\/p>\n<p>Si Ahmed Zennia S., Mati A., Charron C., Cakir-Kiefer C., Kriznik A. &amp;\u00a0<strong>Girardet J.M.\u00a0\u00a0<\/strong>(2019). Effect of nonenzymatic deamidation on the structure stability of\u00a0<em>Camelus dromedarius<\/em>\u00a0alpha-lactalbumin.\u00a0<em>Food Chemistry, 291<\/em>, 207-213. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02095313v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02095313v1<\/strong><\/a><\/p>\n<p><strong>2018<\/strong><\/p>\n<p>Perrot T., Schwartz M., Saiag F., Salzet G., Dumarcay S., Favier F., Gerardin P.,\u00a0<strong>Girardet J.M.<\/strong>, Sormani R., Morel-Rouhier M., Amusant N., Didierjean C. &amp; Gelhaye E. (2018). Fungal glutathione transferases as tools to explore the chemical diversity of Amazonian wood extractives.\u00a0<em>ACS Sustainable Chemistry &amp; Engineering, 6<\/em>, 13078-13085. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02492224v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02492224v1<\/strong><\/a><\/p>\n<p>Mekhaneg B.,\u00a0<strong>Girardet J.M.<\/strong>, Humbert G., Saulnier F., Poirson C. &amp; Bellal M.-M. (2018). Physico-chemical characterization of a milk-clotting fraction extracted from turkey (<em>Meleagris gallopavo<\/em>) proventriculus.\u00a0<em>Innovative Food Science and Emerging Technologies, 48<\/em>, 172-178. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-02621757v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-02621757v1<\/strong><\/a><\/p>\n<p><strong>2017<\/strong><\/p>\n<p>Mati A., Senoussi-Ghezali C., Si Ahmed Zennia S., Almi-Sebbane D., El-Hatmi H. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2017). Dromedary camel milk proteins, a source of peptides having biological activities \u2013 A review<em>. International Dairy Journal,\u00a073,\u00a0<\/em>25-37. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-01611448v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-01611448v1<\/strong><\/a><\/p>\n<p><strong>2016<\/strong><\/p>\n<p>Schwartz M., Didierjean C., Hecker A.,\u00a0<strong>Girardet J.M.<\/strong>, Morel-Rouhier M., Gelhaye E. &amp; Favier F. (2016). Crystal structure of\u00a0<em>Saccharomyces cerevisiae<\/em>\u00a0ECM4, a Xi-class glutathione transferase that reacts with glutathionyl-(hydro)quinones.\u00a0<em>PLOS One, 11<\/em>, e0164678. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-01539425v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-01539425v1<\/strong><\/a><\/p>\n<p>Lallement P.A., Roret T., Tsan P., Gualberto J.M.,\u00a0<strong>Girardet J.M.<\/strong>, Didierjean C., Rouhier N. &amp; Hecker A. (2016). Insights into ascorbate regeneration in plants: Investigating the redox and structural properties of dehydroascorbate reductases from\u00a0<em>Populus trichocarpa<\/em>.\u00a0<em>Biochemical Journal,<\/em>\u00a0<em>473<\/em>, 717-731. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-01287772v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-01287772v1<\/strong><\/a><\/p>\n<p>Guerin J., Kriznik A., Ramalanjaona N., Le Roux Y. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2016). Interaction between dietary bioactive peptides of short length and bile salts in submicellar or micellar state.\u00a0<em>Food Chemistry, 209<\/em>, 114-122. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-01474124v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-01474124v1<\/strong><\/a><\/p>\n<p>El Hatmi H., Jard Z., Khorchani T., Jardin J., Poirson C., Perrin C., Cakir-Kiefer C. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2016). Identification of bioactive peptides derived from caseins, Glycosylation-Dependent Cell Adhesion Molecule-1 (GlyCAM-1), and Peptidoglycan Recognition Protein-1 in fermented camel milk.\u00a0<em>International Dairy Journal<\/em>,\u00a0<em>56<\/em>, 159-168. <a href=\"https:\/\/hal.univ-lorraine.fr\/hal-01278824v1\"><strong>https:\/\/hal.univ-lorraine.fr\/hal-01278824v1<\/strong><\/a><\/p>\n<p><span style=\"color: #800080\"><em><strong>PEER-REVIEWED PUBLICATIONS 1989-2015:<\/strong><\/em><\/span><\/p>\n<p><strong>2015<\/strong><\/p>\n<p>Hafeez Z., Cakir-Kiefer C.,\u00a0<strong>Girardet J.M.<\/strong>, Lecomte X., Paris C., Galia W., Dary A. &amp; Miclo L. (2015). New Insights into the proteolytic system of\u00a0<em>Streptococcus thermophilus<\/em>: Use of isracidin to characterize cell-associated extracellular peptidase activities.\u00a0<em>Journal of Agricultural and Food Chemistry, 63<\/em>, 7522-7531.<\/p>\n<p>Si Ahmed Zennia S., Mati A., Saulnier F., Verdier Y., Chiappetta G., Mulliert G., Miclo L., Vinh J. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2015). Identification by FT-ICR-MS of\u00a0<em>Camelus dromedarius<\/em>\u00a0alpha-lactalbumin variants as the result of nonenzymatic deamidation of Asn-16 and Asn-45.\u00a0<em>Food Chemistry, 187<\/em>, 305-313.<\/p>\n<p>Canabady-Rochelle L.L.S., Harscoat-Schiavo C., Kessler V., Fournier F., Aymes A. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2015). Determination of reducing power and metal chelating ability of antioxidant peptides: Revisited Methods.\u00a0<em>Food Chemistry, 183<\/em>, 129-135.<\/p>\n<p><strong>2014<\/strong><\/p>\n<p>Jrad Z.,\u00a0<strong>Girardet J.M.<\/strong>, Adt I., Oulahal N., Degraeve P., Khorchani T. &amp; El Hatmi H. (2014). Antioxidant activity of camel milk casein before and after\u00a0<em>in vitro<\/em>\u00a0simulated enzymatic digestion.\u00a0<em>Mljekarstvo, 64<\/em>, 287-294.<\/p>\n<p>Jrad Z., El Hatmi H., Adt I.,\u00a0<strong>Girardet J.M.<\/strong>, Cakir-Kiefer C., Jardin J., Degraeve P., Khorchani T. &amp; Oulahal N. (2014). Effect of digestive enzymes on antimicrobial, radical scavenging and angiotensin I-converting enzyme inhibitory activities of camel colostrum and milk proteins.\u00a0<em>Dairy Science and Technology<\/em>,\u00a0<em>94<\/em>, 205-224.<\/p>\n<p>Bunet R., Riclea R., Laureti L., H\u00f4tel L., Paris C.,\u00a0<strong>Girardet J.M.<\/strong>, Spiteller D., Dickschat J.S., Leblond P. &amp; Aigle B. (2014). A single Sfp-type phosphopantetheinyl transferase plays a major role in the biosynthesis of PKS and NRPS derived metabolites in Streptomyces ambofaciens ATCC23877.\u00a0<em>PLOS One<\/em>, 9, e87607.<\/p>\n<p>El Hatmi H., Z. Jrad Z., Khorchani T., Dary A. &amp;\u00a0<strong>Girardet J.M.<\/strong>\u00a0(2014). Fast protein liquid chromatography of camel alpha-lactalbumin fraction with radical scavenging activity.\u00a0<em>Emirates Journal of Food and Agriculture, 26<\/em>, 309-316.<\/p>\n<p><strong>2013<\/strong><\/p>\n<p>Zidane F., Zeder-Lutz G., Altschuh D.,\u00a0<strong>Girardet J.M.<\/strong>, Miclo L., Corbier C. &amp; Cakir-Kiefer C. (2013). Surface plasmon resonance analysis of the binding mechanism of pharmacological and peptidic inhibitors to human somatic angiotensin I-converting enzyme.\u00a0<em>Biochemistry<\/em>,\u00a0<em>52,<\/em>\u00a08722-8731.<\/p>\n<p>Hafeez, Z., Cakir-Kiefer, C.,\u00a0<strong>Girardet, J.M.<\/strong>, Jardin, J., Perrin, C., Dary, A., &amp; Miclo, L. (2013). Hydrolysis of milk-derived bioactive peptides by cell-associated extracellular peptidases of\u00a0<em>Streptococcus thermophilus<\/em>.\u00a0<em>Applied Microbiology and Biotechnology<\/em>, 97, 9787-9799.<\/p>\n<p><strong>2012<\/strong><\/p>\n<p>Ahmad N.,\u00a0<strong>Girardet J.M.<\/strong>, Akbar S., Lanhers M.-C., Paris C., Yen F.T. &amp; Corbier C. (2012). Lactoferrin and its hydrolysate bind directly to the oleate-activated form of the lipolysis stimulated lipoprotein receptor.\u00a0<em>FEBS Journal, 279<\/em>, 4361-4373.<\/p>\n<p>Zidane F., Mat\u00e9os A., Cakir-Kiefer C., Miclo L., Rahuel-Clermont S.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Corbier C. (2012). Binding of divalent metal ions to 1-25 beta-caseinophosphopeptide: an isothermal titration calorimetry study.\u00a0<em>Food Chemistry<\/em>,\u00a0<em>132<\/em>, 391-398.<\/p>\n<p><strong>2011<\/strong><\/p>\n<p>Sadat L., Cakir-Kiefer C., N\u2019Negue M.A., Gaillard J.L.,\u00a0<strong>Girardet J.M.\u00a0<\/strong>&amp; Miclo, L. (2011). Isolation and identification of antioxidative peptides from bovine alpha-lactalbumin.\u00a0<em>International Dairy Journal, 21<\/em>, 214-221.<\/p>\n<p><strong>2010<\/strong><\/p>\n<p>Mat\u00e9os A.,\u00a0<strong>Girardet J.M.<\/strong>, Moll\u00e9 D., Corbier C., Gaillard J.L. &amp; Miclo L. (2010). Identification of phosphorylation sites of equine beta-casein isoforms.\u00a0<em>Rapid Communications in Mass Spectrometry, 24<\/em>, 1533-1542.<\/p>\n<p><strong>Before 2010:<\/strong><\/p>\n<p>Mat\u00e9os A., Miclo L., Moll\u00e9 D., Dary A.,<strong>\u00a0Girardet J.M.\u00a0<\/strong>&amp; Gaillard J.L. (2009). Equine alpha<sub>s1<\/sub>-casein\u00a0: characterization of alternative splicing isoforms and determination of phosphorylation levels.\u00a0<em>Journal of Dairy Science, 92<\/em>, 3604-3615.<\/p>\n<p>Mat\u00e9os A.,\u00a0<strong>Girardet J.M.<\/strong>, Moll\u00e9 D., Dary A., Miclo L. &amp; Gaillard J.L. (2009). Two-dimensional cartography of equine beta-casein variants achieved by isolation of phosphorylation isoforms and control of the deamidation phenomenon.\u00a0<em>Journal of Dairy Science, 92<\/em>, 2389-2399.<\/p>\n<p>Miclo L.,\u00a0<strong>Girardet J.M.<\/strong>, Egito A.S., Moll\u00e9 D., Martin P. &amp; Gaillard J.L. (2007). The primary structure of a low-<em>M<\/em><sub>r<\/sub>\u00a0multi-phosphorylated variant of beta-casein in equine milk.\u00a0<em>Proteomics 7<\/em>, 1327-1335.<\/p>\n<p>Egito A.S.,\u00a0<strong>Girardet J.M.<\/strong>, Laguna L.E., Poirson C., Moll\u00e9 D., Miclo L., Humbert G. &amp; Gaillard J.L. (2007). Milk-clotting activity of enzyme extracts from sunflower and albizia seeds and specific hydrolysis of kappa\u2011casein.\u00a0<em>International Dairy Journal, 17<\/em>, 816-825.<\/p>\n<p>El-Hatmi H.,\u00a0<strong>Girardet J.M.<\/strong>, Gaillard J.L., Yahyaoui M.H. &amp; Attia H. (2007). Characterization of whey proteins of camel (<em>Camelus dromedarius<\/em>) milk and colostrum.\u00a0<em>Small Ruminant Research , 70<\/em>, 267-271.<\/p>\n<p>Egito A.S., Rosinha G.M.S., Laguna L.E., Miclo L.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Gaillard J.L. (2006). [Fast electrophoretic detection method of adulteration of caprine milk by bovine milk].\u00a0<em>Arquivo Brasileiro de Medicina Veterinaria e Zootecnia, 58<\/em>, 932-939.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Miclo L., Florent S., Moll\u00e9 D. &amp; Gaillard J.L. (2006). Determination of the phosphorylation level and deamidation susceptibility of equine beta-casein.\u00a0<em>Proteomics, 6<\/em>, 3707-3717.<\/p>\n<p>N\u2019Negue M.A., Miclo L.,\u00a0<strong>Girardet J.M.<\/strong>, Campagna S., Moll\u00e9 D. &amp; Gaillard J.L. (2006). Proteolysis of bovine alpha-lactalbumin by thermolysin during thermal denaturation.\u00a0<em>International Dairy Journal, 16<\/em>, 1157-1167.<\/p>\n<p>Pang X., Aigle B.,\u00a0<strong>Girardet J.M.<\/strong>, Mangenot S., Pernodet J.L., Decaris B. &amp; Leblond P. (2004). Functional angucycline-like antibiotic gene cluster in the terminal inverted repeats of the\u00a0<em>Streptomyces ambofaciens<\/em>\u00a0linear chromosome.\u00a0<em>Antimicrobial Agents and Chemotherapy, 48<\/em>, 575-588.<\/p>\n<p>Nabhan M.A.,\u00a0<strong>Girardet J.M.<\/strong>, Campagna S., Gaillard J.L. &amp; Le Roux Y. (2004). Isolation and characterization of co-polymers of beta-lactoglobulin, alpha-lactalbumin, kappa-casein, and alpha<sub>s1<\/sub>-casein generated by pressurization and thermal treatment of raw milk.\u00a0<em>Journal of Dairy Science, 87<\/em>, 3614-3622.<\/p>\n<p>Campagna S., Mathot A.G., Fleury Y.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Gaillard J.L. (2004). Antibacterial activity of lactophoricin, a synthetic 23-residues peptide derived from the sequence of bovine milk component-3 of proteose peptone.\u00a0<em>Journal of Dairy Science, 87<\/em>, 1621-1626.<\/p>\n<p><strong>Girardet J.M.<\/strong>, N\u2019Negue M.A., Egito A.S., Campagna S., Lagrange A. &amp; Gaillard J.L. (2004). Multiple forms for equine alpha\u2011lactalbumin: evidence of N-glycosylated and deamidated forms.\u00a0<em>International Dairy Journal, 14<\/em>, 207-217.<\/p>\n<p>Egito A.S.,\u00a0<strong>Girardet J.M.<\/strong>, Poirson C., Moll\u00e9 D., Humbert G., Miclo L. &amp; Gaillard J.L. (2003). Action of plasmin on equine beta\u2011casein.\u00a0<em>International Dairy Journal, 13<\/em>, 813-820.<\/p>\n<p>Moussaoui F., Laurent F.,\u00a0<strong>Girardet J.M.<\/strong>, Humbert G., Gaillard J.L. &amp; Le Roux Y. (2003). Characterization and proteolytic origins of specific peptides appearing during lipopolysaccharide experimental mastitis.\u00a0<em>Journal of Dairy Science, 86<\/em>, 1163-1170.<\/p>\n<p>Gelhaye E., Rouhier N., Vlamis-Gardikas A.,\u00a0<strong>Girardet J.M.<\/strong>, Sauti\u00e8re P.E., Sauzet M., Martin F. &amp; Jacquot J.P. (2003). Identification and characterization of a third thioredoxin\u00a0<em>h<\/em>\u00a0in poplar.\u00a0<em>Plant Physiology and Biochemistry, 41<\/em>, 629-635.<\/p>\n<p>Egito A.S., Miclo L., Lopez C., Adam A.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Gaillard J.L. (2002). Separation and characterization of mares\u2019 milk alpha<sub>s1<\/sub>-, beta-, kappa-caseins, gamma-casein-like, and proteose peptone component 5-like peptides.\u00a0<em>Journal of Dairy Science, 85<\/em>, 697-706.<\/p>\n<p>Egito A.S., Haussard M., Poirson C.,\u00a0<strong>Girardet J.M.<\/strong>, Miclo L. &amp; Gaillard J.L. (2002) Angiotensin I-converting enzyme inhibitory properties of an equine tryptic digest and characterisation of some active peptides.\u00a0<em>In Peptides 2002 pp. 92-93 (Ettore Benedetti and Carlo Pedone, Eds.), Edizioni Ziino, Napoli, Italia.<\/em><\/p>\n<p>Egito A.S.,\u00a0<strong>Girardet J.M.<\/strong>, Miclo L., Moll\u00e9 D., Humbert G. &amp; Gaillard J.L. (2001). Susceptibility of equine kappa- and beta-caseins to hydrolysis by chymosin.\u00a0<em>International Dairy Journal, 11<\/em>, 885-893.<\/p>\n<p>Egito A.S.,\u00a0<strong>Girardet J.M.<\/strong>, Miclo L. &amp; Gaillard J.L. (2001). Highly sensitive periodic acid\/Schiff detection of bovine milk glycoproteins electrotransferred after nondenaturing electrophoresis, urea electrophoresis, and isoelectric focusing.\u00a0<em>Le Lait, 81<\/em>, 775-785.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Humbert G., Creusot N., Chardot V., Campagna S., Courthaudon J.L. &amp; Gaillard J.L. (2001). Dilational rheology of mixed beta-casein\/Tween 20 and beta-casein (f114-169)\/Tween 20 films at oil-water interface.\u00a0<em>Journal of Colloid and Interface Science, 243<\/em>, 515-522.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Debomy L., Courthaudon J.L., Miclo L., Humbert G. &amp; Gaillard J.L. (2000). Viscoelastic properties of oil-water interfaces covered by bovine beta-casein tryptic peptides.\u00a0<em>Journal of Dairy Science, 83<\/em>, 2410-2421.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Saulnier F., Gaillard J.L., Ramet J.P. &amp; Humbert G. (2000). Camel (<em>Camelus dromedarius<\/em>) milk PP3: evidence for an insertion in the amino-terminal sequence of the camel milk whey protein.\u00a0<em>Biochemistry and Cell Biology, 78<\/em>, 19-26.<\/p>\n<p>Courthaudon J.L.,\u00a0<strong>Girardet J.M.<\/strong>, Campagne S., Rouhier L.M., Campagna S., Lorient D. &amp; Linden G. (1999). Surface active and emulsifying properties of casein micelles compared to those of sodium caseinate.\u00a0<em>International Dairy Journal, 9<\/em>, 411-412.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Courthaudon J.L., Campagna S., Puyjalon V., Lorient D. &amp; Linden G. (1999). Proteolysis of milk casein micelle and sodium caseinate in oil-in-water emulsion.\u00a0<em>International Dairy Journal, 9<\/em>, 409-410.<\/p>\n<p>Montagne L.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Humbert G. (1999). Amino-terminal sequencing of the ovine milk fat globule membrane protein butyrophilin.\u00a0<em>Le Lait, 79<\/em>, 275-279.<\/p>\n<p>Campagna S., Vitoux B., Humbert G.,\u00a0<strong>Girardet J.M.<\/strong>, Linden G., Haertle T. &amp; Gaillard\u00a0J.L. (1998). Conformational studies of a synthetic peptide from the putative lipid-binding domain of bovine milk component PP3.\u00a0<em>Journal of Dairy Science, 81<\/em>, 3139-3148.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Saulnier F., Linden G. &amp; Humbert G. (1998). Rapid separation of bovine whey proteins by membrane convective liquid chromatography, perfusion chromatography, continuous bed chromatography, and capillary electrophoresis.\u00a0<em>Le Lait, 78<\/em>, 391-400.<\/p>\n<p>Coddeville B.,\u00a0<strong>Girardet J.M.<\/strong>, Plancke Y., Campagna S., Linden G. &amp; Spik G. (1998), Structures of the O\u2011glycopeptides isolated from bovine milk component PP3.\u00a0<em>Glycoconjugate Journal, 15<\/em>, 371-378.<\/p>\n<p>Guimont C., Marchal E.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Linden G. (1997). Biological active factors in bovine milk and dairy by-products: influence on cell culture.\u00a0<em>Critical Reviews in Food Science and Nutrition, 37<\/em>, 393-410.<\/p>\n<p>Rudolf E.,\u00a0<strong>Girardet J.M.<\/strong>, Bautz A.M. &amp; Dournon C. (1997). Purification and partial characterization of peptidase-1, a sex-linked enzyme in\u00a0<em>Pleurodeles waltl<\/em>\u00a0(urodele amphibian).\u00a0<em>Biochemistry and Cell Biology, 75<\/em>, 803-806.<\/p>\n<p>Bernos E.,\u00a0<strong>Girardet J.M.<\/strong>, Humbert G. &amp; Linden G. (1997). Role of the O\u2011phosphoserine clusters in the interaction of the bovine milk alphas1\u2011, beta\u2011, kappa\u2011caseins and the PP3 component with immobilized iron(III) ions.\u00a0<em>Biochimica et Biophysica Acta (Protein Structure and Molecular Enzymology), 1337<\/em>, 149\u2011159.<\/p>\n<p><strong>Girardet J.M.<\/strong>\u00a0&amp; Linden G. (1996). PP3 component of bovine milk: a phosphorylated whey glycoprotein.\u00a0<em>Journal of Dairy Research, 63<\/em>, 333-350.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Coddeville B., Plancke Y., Strecker G., Campagna S. &amp; Linden G. (1995). Structure of glycopeptides isolated from bovine milk component PP3.\u00a0<em>European Journal of Biochemistry (devenu FEBS Journal), 234<\/em>, 939-946.<\/p>\n<p>Le\u00a0Roux Y.,\u00a0<strong>Girardet J.M.<\/strong>, Humbert G., Laurent F. &amp; Linden G. (1995). Proteolysis in samples of quarter milk with varying somatic cell counts.\u00a02. component PP3 and beta-CN\u20111P(f29\u2011105 and f29\u2011107) of the proteose-peptone fraction.\u00a0<em>Journal of Dairy Science, 78<\/em>, 1298-1305.<\/p>\n<p>Courthaudon J.L.,\u00a0<strong>Girardet J.M.<\/strong>, Chapal C., Lorient D. &amp; Linden G. (1995) Surface activity and competitive adsorption of milk component-3 and porcine pancreatic lipase at the dodecane-water interface.\u00a0<em>In Food Macromolecules and Colloids, pp.\u00a058\u201170 (Ed. E. Dickinson) London: Royal Society of Chemistry.<\/em><\/p>\n<p>Etienne L.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Linden G. (1994). Growth promotion of\u00a0<em>Bifidobacterium animalis<\/em>\u00a0by bovine milk proteose-peptone.\u00a0<em>Le Lait, 74<\/em>, 313\u2011323.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Saulnier F., Driou A., Linden G., Coddeville B. &amp; Spik G. (1994). High performance electrophoresis chromatography of bovine milk component\u20113 glycoproteins.\u00a0<em>Journal of Dairy Science, 77<\/em>, 1205\u20111216.<\/p>\n<p>Mati A., Moulti-Mati F.,\u00a0<strong>Girardet J.M.<\/strong>, Fokou E., Belleville-Nabet F., Nabet P. &amp; Linden\u00a0G. (1993). Mitogenic activity of hydrophobic fractions of proteose-peptone from cows\u2019, ewes\u2019 and goats\u2019 milk measured with MARK\u00a03 hybridoma culture.\u00a0<em>Journal of Dairy Research, 60<\/em>, 443\u2011448.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Linden G., Loye S., Courthaudon J.L. &amp; Lorient D. (1993). Study of mechanism of lipolysis inhibition by bovine milk proteose-peptone component\u20113.\u00a0<em>Journal of Dairy Science, 76<\/em>, 2156\u20112163.<\/p>\n<p>Mati A.,\u00a0<strong>Girardet J.M.<\/strong>, Xenakis D. &amp; Linden G. (1991). Isolement et caract\u00e9risation de la fraction hydrophobe des prot\u00e9ose-peptones des laits bovin, ovin et caprin.\u00a0<em>Le Lait, 71<\/em>, 259\u2011273.<\/p>\n<p>Saulnier F., Ferrero F., Choukri A.,\u00a0<strong>Girardet J.M.<\/strong>\u00a0&amp; Linden G. (1991). Estimation de la d\u00e9naturation des prot\u00e9ines par spectrofluorim\u00e9trie d\u2019absorption mol\u00e9culaire\u00a0: applications aux lactos\u00e9rums industriels.\u00a0<em>Le Lait, 71<\/em>, 511\u2011518.<\/p>\n<p><strong>Girardet J.M.<\/strong>, Mati A., Sanogo T., Etienne L. &amp; Linden G. (1991). Fast protein liquid chromatography purification of hydrophobic fraction of bovine milk proteose-peptone and characterization by bidimensional electrophoresis.\u00a0<em>Journal of Dairy Research, 58<\/em>, 85\u201198.<\/p>\n<p><strong>Girardet J.M.<\/strong>, P\u00e2quet D. &amp; Linden G. (1989). Effects of chromatographic parameters on the fractionation of whey proteins by anion exchange FPLC.\u00a0<em>Milchwissenschaft, 44<\/em>, 692\u2011696.<\/p>\n<p><span style=\"color: #800080\"><strong><em>INVITED LECTURES:<\/em><\/strong><\/span><\/p>\n<p><strong>Girardet J.M.<\/strong>\u00a0(2014). Milk proteins as source of biofunctional peptides [Les prot\u00e9ines laiti\u00e8res sources de peptides biofonctionnels]. 1<sup>er<\/sup>\u00a0Congr\u00e8s International de Technologies Alimentaires et Contr\u00f4le Qualit\u00e9 des Aliments \u201cAGROINNOV\u00a0: Technologies Innovantes pour la Production Alimentaire\u201d, Djerba, Tunisia, April, 25 \u2013 27, 2014.<\/p>\n<p><strong>Girardet J.M.<\/strong>\u00a0(2011). Antioxidant peptides from milk, unveiling and production by lactic acid bateria [Les peptides antioxydants du lait, leur mise en \u00e9vidence et leur production par une bact\u00e9rie lactique]. Antioxydants 2011 : Biodisponibilit\u00e9, M\u00e9tabolomique &amp; Innovations Strat\u00e9giques. Soci\u00e9t\u00e9 Fran\u00e7aise des Antioxydants (SFA), Paris, France, June, 09, 2011.<\/p>\n<p>&nbsp;<\/p>\n","protected":false},"excerpt":{"rendered":"<p>PAST AND CURRENT FUNCTIONS: \u2013 2015: Currently assigned to UMR 1136 INRAE\/University of Lorraine IAM as Research Engineer. Manager of the &#8216;Structural and Functional Approaches of Cellular InterActions&#8217; (ASIA) platform located at the Faculty of Sciences and Technologies: https:\/\/a2f.univ-lorraine.fr\/asia\/ \u2013 &hellip; <a href=\"https:\/\/mycor.iam.inrae.fr\/IAM\/?page_id=4396\">Continue reading <span class=\"meta-nav\">&rarr;<\/span><\/a><\/p>\n","protected":false},"author":7,"featured_media":0,"parent":850,"menu_order":0,"comment_status":"closed","ping_status":"open","template":"","meta":{"footnotes":""},"class_list":["post-4396","page","type-page","status-publish","hentry"],"_links":{"self":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/4396","targetHints":{"allow":["GET"]}}],"collection":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/users\/7"}],"replies":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fcomments&post=4396"}],"version-history":[{"count":12,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/4396\/revisions"}],"predecessor-version":[{"id":13144,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/4396\/revisions\/13144"}],"up":[{"embeddable":true,"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=\/wp\/v2\/pages\/850"}],"wp:attachment":[{"href":"https:\/\/mycor.iam.inrae.fr\/IAM\/index.php?rest_route=%2Fwp%2Fv2%2Fmedia&parent=4396"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}