AOAC SPIFAN Stakeholder Panel Meeting Book (September 7, 2019)

References

General information, amongst others from:

X Baker, E. N., & Baker, H. M. (2005). Molecular structure, binding properties and dynamics of lactoferrin. Cellular and Molecular Life Sciences , 62 (22), 2531–2539. https://doi.org/10.1007/s00018-005-5368-9 X Billakanti, J., McRae, J., Mayr, M., & Johnson, K. (2019). Advanced analytical tools for bovine lactoferrin identification and quantification in raw skim milk to finished lactoferrin powders. International Dairy Journal , 104546. https://doi.org/10.1016/j.idairyj.2019.104546 X Bokkhim, H., Bansal, N., Grndahl, L., & Bhandari, B. (2013). Physico-chemical properties of different forms of bovine lactoferrin. Food Chemistry , 141 (3), 3007–3013. https://doi.org/10.1016/j.foodchem.2013.05.139

X Brock, J. H. (2012). Lactoferrin – 50 years on. Biochemistry and Cell Biology , 90 (3), 245–251. https://doi.org/10.1139/o2012-018

X Demmelmair, H., Prell, C., Timby, N., & Lönnerdal, B. (2017). Benefits of lactoferrin, osteopontin and milk fat globule membranes for infants. Nutrients , 9 (8), 1–22. https://doi.org/10.3390/nu9080817 X Franco, I., Pérez, M. D., Conesa, C., Calvo, M., & Sánchez, L. (2018). E ff ect of technological treatments on bovine lactoferrin : An overview A ) B ) C ), 106 (December 2017), 173–182. https://doi.org/10.1016/j.foodres.2017.12.016

X Lonnerdal, B; Iyer, S. (1995). LACTOFERRIN : MOLECULAR STRUCTURE AND BIOLOGICAL FUNCTION. Annual Reviews Nutrition , 15 , 93–110.

X Sreedhara, A. (2011). Structure, stability and digestion of caprine and bovine lactoferrin, a comparative study .

X Parc AL, Karav S, Rouquié C, Maga EA, Bunyatratchata A, Barile D (2017) Characterization of recombinant human lactoferrin N -glycans expressed in the milk of transgenic cows. PLoS ONE 12(2): e0171477. https://doi.org/10.1371/journal.pone.0171477 X Le Parc A, Dallas DC, Duaut S, Leonil J, Martin P, Barile D. Characterization of goat milk lactoferrin N-glycans and comparison with the N- glycomes of human and bovine milk. Electrophoresis . 2014;35(11):1560–1570. doi:10.1002/elps.201300619 X Karav S, German JB, Rouquié C, Le Parc A, Barile D. Studying Lactoferrin N-Glycosylation. Int J Mol Sci . 2017;18(4):870. Published 2017 Apr 20. doi:10.3390/ijms18040870 X Rosa L, Cutone A, Lepanto MS, Paesano R, Valenti P. Lactoferrin: A Natural Glycoprotein Involved in Iron and Inflammatory Homeostasis. Int J Mol Sci . 2017;18(9):1985. Published 2017 Sep 15. doi:10.3390/ijms18091985

References

Method references:

X Billakanti, J., McRae, J., Mayr, M., & Johnson, K. (2019). Advanced analytical tools for bovine lactoferrin identification and quantification in raw skim milk to finished lactoferrin powders. International Dairy Journal , 104546. https://doi.org/10.1016/j.idairyj.2019.104546 X Campanella, L., Martini, E., Pintore, M., & Tomassetti, M. (2009). Determination of lactoferrin and immunoglobulin G in animal milks by new immunosensors. Sensors , 9 (3), 2202–2221. https://doi.org/10.3390/s90302202 X Chen, Z., Li, H., Jia, W., Liu, X., Li, Z., Wen, F., … Xu, D. (2017). Bivalent Aptasensor Based on Silver-Enhanced Fluorescence Polarization for Rapid Detection of Lactoferrin in Milk. Analytical Chemistry , 89 (11), 5900–5908. https://doi.org/10.1021/acs.analchem.7b00261 X Davis, S. R., & South, C. R. (2015). Suspension of milking in dairy cows produces a transient increase in milk lactoferrin concentration and yield after resumption of milking. Journal of Dairy Science , 98 (11), 7823–7830. https://doi.org/10.3168/jds.2015-9772 X Dračková, M., Borkovcová, I., Janštová, B., Naiserová, M., Přldalová, H., Navrátilová, P., & Vorlová, L. (2009). Determination of lactoferrin in goat milk by HPLC method. Czech Journal of Food Sciences , 27 (SPEC. ISS.). X Ellingson, D. J., Shippar, J. J., Vennard, T. R., Moloney, C., O’Connor, D., O’Regan, J., … Affolter, M. (2019). Analytical method for lactoferrin in milk-based infant formulas by signature peptide quantification with ultra-high performance LC- tandem mass spectrometry. Journal of AOAC International , 102 (3), 915–925. https://doi.org/10.5740/jaoacint.18-0226 X Feng, P., Fuerer, C., & McMahon, A. (2017). Quantification of whey protein content in infant formulas by sodium dodecyl sulfate-capillary gel electrophoresis (SDS-CGE): Single-laboratory validation, first action 2016.15. Journal of AOAC International , 100 (2), 510–521. https://doi.org/10.5740/jaoacint.16-0344 X Hiss, S., Meyer, T., & Sauerwein, H. (2008). Lactoferrin concentrations in goat milk throughout lactation. Small Ruminant Research , 80 (1–3), 87–90. https://doi.org/10.1016/j.smallrumres.2008.07.027 X Indyk, H. E., Filonzi, E. L., & Gapper, L. W. (2005). Determination of lactoferrin in bovine milk, colostrum and infant formulas by optical biosensor analysis. International Dairy Journal , 15 (3), 429–438. https://doi.org/10.1016/j.idairyj.2004.09.003