Primary proteolysis studied in a cast cheese made from microfiltered milk |
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| Affiliation: | 1. Arla Foods Innovation, Rørdrumvej 2, 8220 Brabrand, Denmark;2. Department of Food Science, Dairy Technology, Centre for Advanced Food Studies, The Royal Veterinary and Agricultural University, Rolighedsvej 30, 1958 Frederiksberg C, Denmark;3. Department of Food Technology, Engineering and Nutrition, Lund University, P.O. Box 124, 221 00 Lund, Sweden;1. Department of Food and Nutritional Sciences, University College Cork, Ireland;1. University of Copenhagen, Department of Food Science, Rolighedsvej 30, 1958 Frederiksberg C, Denmark;2. Haramaya University, School of Animal and Range Sciences, P.O.Box: 138, Dire Dawa, Ethiopia;3. Technical University of Denmark, National Food Institute, 2860, Søborg, Denmark;4. Botswana University of Agriculture and Natural Resources, Department of Food Science and Technology, Private Bag 0027, Gaborone, Botswana;1. Arla Foods Strategic Innovation Centre, Rørdrumvej 2, DK-8220 Brabrand, Denmark;2. Aarhus University, Dept. of Food Science, Faculty of Science and Technology, Blichers Allé 20, DK-8830 Tjele, Denmark;3. Arla Foods Strategic Innovation Centre, Lindhagensgatan 126, SE-10546 Stockholm, Sweden;4. University of Copenhagen, Department of Food Science, Rolighedsvej 30, DK-1958 Frederiksberg C, Denmark;5. Dept of Food Technology, Engineering and Nutrition, Lund University, SE-22100 Lund, Sweden;1. Laboratoire d’Elevage et Faune Sauvage, Institut des Régions Arides de Médenine, Tunisia;2. Département Agro-Alimentaire, Institut Supérieur de Biologie Appliquée de Médenine, Université de Gabes, Tunisia;3. INRA, UMR1253 Science et Technologie du Lait et de l''Œuf, F-35042, Rennes, France;4. Agrocampus Ouest, UMR1253 Science et Technologie du Lait et de l''Œuf, F-35042, Rennes, France;5. Université de Lorraine, Unité de Recherche Animal et Fonctionnalités des Produits Animaux (UR AFPA), Équipe Protéolyse et Biofonctionnalités des Protéines et des Peptides (PB2P Team), Vandœuvre-lès-Nancy, F-54506, France;6. INRA, UR AFPA USC 340, Vandœuvre-lès-Nancy, F-54506, France;1. Department of Life Sciences, University of Modena and Reggio Emilia, Via Amendola, 2 – Pad. Besta, 42100 Reggio Emilia, Italy;2. Department of Food and Dairy Sciences and Technology, Damanhour University, 22516 Damanhour, Egypt;1. School of Food and Health, Beijing Technology and Business University, Beijing 100048, China;2. Junlebao Dairy Group Co.,Ltd., Shijiazhuang, Hebei 050221, China;3. School of Food and Nutritional Sciences, University College Cork, Cork, Ireland;1. Teagasc Food Research Centre, Moorepark, Fermoy, Co. Cork, Ireland;2. School of Food and Nutritional Sciences, University College, Cork, Ireland |
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| Abstract: | Primary proteolysis was studied in a starter-free cheese model made from microfiltered (MF) milk (19.0% casein,<0.2% whey proteins). Specificity of plasmin and chymosin activity was investigated in the pH range 5.0–6.0, by analysis of peptide composition using high-performance liquid chromatography and liquid chromatography–mass spectrometry. Hydrolysis experiments with purified caseins were performed to aid identification of peptides released by specific activities. Plasmin had no activity in cheese below pH 5.4, while its activity increased from pH 5.4 to 6.0. Chymosin activity on the Phe23–Phe24 bond of αS1-casein had an optimum pH around 5.3, while release of the bitter peptide β-casein (f193–209), effected by chymosin, was highest at pH 6.0. At pH <5.3, the specificity of chymosin on αS1-casein changed, and the peptide bond Leu20–Leu21 was cleaved at an increasing rate with decreasing pH. Demineralisation of the MF retentate generally increased proteolytic activity. |
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