Influence of pH on retention of camel chymosin in curd |
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| Affiliation: | 1. Department of Food Science, Faculty of Science, University of Copenhagen, Rolighedsvej 30, 1958 Frederiksberg, Denmark;2. Chr. Hansen A/S, 2970 Hørsholm, Denmark;1. Department of Food Technology (DTA), School of Food Engineering (FEA), University of Campinas (UNICAMP), Monteiro Lobato, 80, PO Box 6121, 13083–862, Campinas, SP, Brazil;2. Center of Studies and Researches in Food (NEPA), University of Campinas (UNICAMP), Albert Einstein, 291, 13083-852, Campinas, SP, Brazil;1. Department of Food Quality and Nutrition, Research and Innovation Centre, Fondazione Edmund Mach 1, 38010 San Michele all’Adige, Italy;2. Unit of Computational Biology, Research and Innovation Centre, Fondazione Edmund Mach 1, 38010 San Michele all’Adige, Italy;3. Caglificio Clerici S.p.A. and Sacco S.r.l, Via Manzoni 29, I-22071 Cadorago (CO), Italy;4. Caglio Bellucci S.r.l, Via Vito Bering 57, 41123 Modena (MO), Italy;1. STLO, UMR 1253, INRA, Agrocampus Ouest, 35000 Rennes, France;2. Agrocampus Ouest, 65 rue de St-Brieuc, 35042 Rennes Cedex, France;3. Faculté d’Agronomie et des Sciences de l’Environnement, Université Dandicko Dankoulodo de Maradi, BP 465 ADS Maradi, Niger;1. Tecnología de los Alimentos, Universidad de Zaragoza, Miguel Servet, 177, 50013 Zaragoza, Spain;2. Nutrición y Bromatología, Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet, 177, 50013 Zaragoza, Spain |
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| Abstract: | Retained coagulant in cheese initiates casein breakdown and influences cheese structure and flavour formation. This study investigated the influence of milk pH on retention of camel chymosin in curd and compared it with bovine chymosin. Milk at five different pH levels was coagulated with same coagulant activity of each chymosin and centrifuged. Chymosin activity in whey was determined using the synthetic peptide Pro-Thr-Glu-Phe-(NO2-Phe)-Arg-Leu as substrate and HPLC analysis of the resulting product. Camel chymosin had 2.7 times lower activity in milk than bovine chymosin at the same coagulation activity. The retention of camel chymosin in curd was rather constant at ∼20% between pH 6.65 and 6.00, while it increased almost linear from 2 to 21% for bovine chymosin. The lower pH dependence for retention of camel chymosin than of bovine chymosin may be explained by a lower negative charge of the camel chymosin molecule. |
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