Effect of photo-oxidation of major milk proteins on protein structure and hydrolysis by chymosin |
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| Authors: | Trine K. Dalsgaard Lotte B. Larsen |
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| Affiliation: | 1. Analytical Chemistry and Biomedicine Group, Pharmaceuticals Sciences Faculty, Campus of Zaragocilla, University of Cartagena, 130015 Cartagena, Colombia;2. Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Avenue Agustín Escardino 7, 46980 Paterna, Valencia, Spain;1. Department of Food Science, Faculty of Science and Technology, Aarhus University, PO Box 50, DK-8830 Tjele, Denmark;2. Laboratory of Toxicology and Pharmacology, National Institutes of Health, Research Triangle Park, NC 27709, USA;3. Laboratory of Structural Biology, National Institute of Environmental Health Sciences, National Institutes of Health, Research Triangle Park, NC 27709, USA;4. Arla Foods, Strategic Innovation Centre, Rørdrumvej 2, DK-8220 Brabrand, Denmark;1. Programa de Pós Graduação em Ciências Farmacêuticas, Núcleo de Investigações Químico-Farmacêuticas (NIQFAR), Universidade do Vale do Itajai (UNIVALI) – Campus Itajaí, Rua Uruguai, 458, Centro CEP: 88302-901, Santa Catarina, Brazil;2. School of Pharmaceutical Sciences of Ribeirão Preto of the University of São Paulo, Avenida do Café, s/n, 14040-903 Ribeirão Preto, SP, Brazil;1. Departamento de Química Física, Facultad de Química, Pontificia Universidad Católica de Chile, Santiago, Chile;2. Facultad de Química y Biología, Universidad de Santiago de Chile (USACH), Santiago, Chile;3. Department of Biomedical Sciences, Panum Institute, University of Copenhagen, Denmark;1. URPhyM-Laboratoire de Chimie Physiologique, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium;2. URPhyM-Laboratoire de Physiologie et Pharmacologie, Narilis, University of Namur, 61 rue de Bruxelles, 5000 Namur, Belgium |
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| Abstract: | Changes in the protein structure of different major milk proteins in response to photo-oxidation and its effect on hydrolysis by chymosin were studied by determination of free amino-terminal groups and by peptide mapping using liquid chromatography coupled with mass spectrometry. Changes were seen in the formation of peptides by chymosin after photo-oxidation of all substrates studied, but the extent of changes varied between the different substrates. Oxidative changes involving tryptophan residues and formation of dityrosines were high in the casein, and conformational changes of both αS- and β-casein were indicated by changes in the micro-environment of the tryptophan residues after oxidation. A decreased accessibility of chymosin to oxidized caseins was reflected in a lower overall level of free amino-terminal groups, and changed peptide maps. Although β-lactoglobulin and lactoferrin showed marginal conformational changes, a higher level of free amino-terminal groups was observed, and a range of peptides were found to increase for these two proteins. |
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