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The Heat Stability of Indigenous and Bacterial Enzymes in Milk

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Agents of Change

Part of the book series: Food Engineering Series ((FSES))

Abstract

This chapter focuses on the heat stability of indigenous (expressed from different bovine tissues and cells, then secreted into milk) and bacterial (exogenous) dairy enzymes as well as thermal and non-thermal inactivation methods. The fundamentals of heat inactivation kinetics are outlined and the heat stabilities of the following enzymes are discussed in detail: alkaline phosphatase, γ-glutamyltransferase, lactoperoxidase, lipoprotein lipase, cathepsin D, plasmin, and peptidases from Pseudomonas ssp. Based on the presented kinetic data of these enzymes, inactivation lines revealing possible temperature-time combinations for a targeted inactivation were calculated. The given information should serve as a base to deduce individual parameters (e.g., time and temperature) for handling each dairy derived enzyme.

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Author information

Authors and Affiliations

  1. Department of Soft Matter Science and Dairy Technology, Institute of Food Science and Biotechnology, University of Hohenheim, Stuttgart, Germany

    Britta Graf, Johannes Schäfer, Zeynep Atamer & Jörg Hinrichs

Authors
  1. Britta Graf
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  2. Johannes Schäfer
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  3. Zeynep Atamer
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  4. Jörg Hinrichs
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Correspondence to Jörg Hinrichs .

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Editors and Affiliations

  1. School of Food and Nutritional Sciences, University College Cork, Cork, Cork, Ireland

    Alan L. Kelly

  2. Department of Food Science, Aarhus University, Aarhus, Denmark

    Lotte Bach Larsen

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Graf, B., Schäfer, J., Atamer, Z., Hinrichs, J. (2021). The Heat Stability of Indigenous and Bacterial Enzymes in Milk. In: Kelly, A.L., Larsen, L.B. (eds) Agents of Change. Food Engineering Series. Springer, Cham. https://doi.org/10.1007/978-3-030-55482-8_12

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