The milk acid proteinase cathepsin D: a review |
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| Affiliation: | 1. Department of Food Science and Technology, University College, Cork, Ireland;2. Department of Animal Product Quality, Danish Institute of Agricultural Sciences, P.O. Box 50, DK-8830 Tjele, Denmark;1. Fonterra Research and Development Centre, Private Bag 11029, Palmerston North 4442, New Zealand;2. Massey Institute of Food Science and Technology, Massey University, Private Bag 11222, Palmerston North 4442, New Zealand;3. Dairy Foods Research and Development, Land O''Lakes, Inc., MN, USA;1. Department of Food Science, Aarhus University, 8200 Aarhus N, Denmark;2. Arla Foods Ingredients, 6920 Videbæk, Denmark;1. Universität Hohenheim, Institute of Food Science and Biotechnology, Department of Soft Matter Science and Dairy Technology, Garbenstr. 21, 70599 Stuttgart, Germany;2. Universität Hohenheim, Institute of Food Science and Biotechnology, Department of Biotechnology and Enzyme Science, Garbenstr. 25, 70599 Stuttgart, Germany;3. Technische Universität München, Wissenschaftszentrum Weihenstephan, Zentralinstitut für Ernährungs- und Lebensmittelforschung (ZIEL), Lehrstuhl für Mikrobielle Ökologie, Weihenstephaner Berg 3, 85354 Freising, Germany;1. National R & D Center for Freshwater Fish Processing, and Engineering Research Center of Freshwater Fish High-value Utilization of Jiangxi Province, College of Life Science, Jiangxi Normal University, Nanchang, Jiangxi 330022, China;2. State Key Laboratory of Food Science and Technology, Nanchang University, Nanchang, Jiangxi 330047, China;1. Department of Food Technology, Universidade Federal de Viçosa (UFV) Avenida P. H. Rolfs, Viçosa, MG, 36570-900, Brazil;2. Department of Food Science, School of Food Engineering, Universidade de Campinas (Unicamp) Rua Monteiro Lobato, 80, Campinas, SP, 13083-862, Brazil;3. Center of Natural Sciences, Universidade Federal de São Carlos (UFSCar), Buri, SP, 18290-000, Brazil;4. STLO, Agrocampus Ouest, UMR1253, INRA, 65 rue de Saint Brieuc, 35042, Rennes, France;5. Department of Physics, Universidade Federal de Viçosa (UFV) Avenida P. H. Rolfs, Viçosa, MG, 36570-900, Brazil |
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| Abstract: | Cathepsin D is a lysosomal aspartic proteinase with a low pH optimum, found in many tissues and in bovine milk. It is synthesised as its inactive zymogen, procathepsin D. Procathepsin D can convert itself, by an autoproteolytic pathway, into an active intermediate, pseudocathepsin D, while other proteases are involved in the processing to mature cathepsin D. Cathepsin D is known to participate in a range of physiological processes. Pro-, pseudo- and mature cathepsin D have been purified from bovine milk, but procathepsin D is the major form present in milk. Cathepsin D activity in milk appears correlated with somatic cell count. The active forms of the enzyme readily hydrolyse αS1-, αS2- and β-caseins, in the case of αS1-casein and β-casein with a specificity similar to that of chymosin. Cathepsin D can also produce para-κ-casein from κ-casein and, at high concentrations, can coagulate milk. Cathepsin D appears to be able to at least partially survive commercial pasteurisation processes. In recent years, increasing evidence has been documented indicating a role for this enzyme in proteolysis in cheese during ripening, most clearly in cheese where rennet activity is low, such as Swiss cheese, Quarg and Feta. Further research is required to evaluate the significance of this enzyme in more detail. |
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