Food physical chemistry is considered to be a branch of Food chemistry[1][2] concerned with the study of both physical and chemical interactions in foods in terms of physical and chemical principles applied to food systems, as well as the applications of physical/chemical techniques and instrumentation for the study of foods.[3][4][5][6] This field encompasses the "physiochemical principles of the reactions and conversions that occur during the manufacture, handling, and storage of foods."[7]
Food physical chemistry concepts are often drawn from rheology, theories of transport phenomena, physical and chemical thermodynamics, chemical bonds and interaction forces, quantum mechanics and reaction kinetics, biopolymer science, colloidal interactions, nucleation, glass transitions, and freezing,[8][9] disordered/noncrystalline solids.
Understanding food processes and the properties of foods requires a knowledge of physical chemistry and how it applies to specific foods and food processes. Food physical chemistry is essential for improving the quality of foods, their stability, and food product development. Because food science is a multi-disciplinary field, food physical chemistry is being developed through interactions with other areas of food chemistry and food science, such as food analytical chemistry, food process engineering/food processing, food and bioprocess technology, food extrusion, food quality control, food packaging, food biotechnology, and food microbiology.
Carbohydrates structure and interactions with water and proteins
Maillard browning reactions
Lipids structures and interactions with water and food proteins
Food proteins structure, hydration and functionality in foods
Food protein denaturation
Food enzymes and reaction mechanisms
Vitamin interactions and preservation during food processing
Interaction of salts and minerals with food proteins and water
Color determinations and food grade coloring
Flavors and sensorial perception of foods
Properties of food additives
Related fields
Visualisation of the human interactome network topology with the blue lines between proteins (represented as points) showing protein-protein interactions
Example of a GC-MS instrumentAn FTIR interferogram. The central peak is at zero retardation, ZPD) where the maximum amount of light passes through the interferometer to the detector.
↑Abragam, A.; Bleaney, B. Electron paramagnetic resonance of transition ions. Clarendon Press:Oxford, 1970, 1,116 pages.
↑Physical Chemistry of Food Processes, Advanced Techniques, Structures and Applications.1994. van Nostrand-Reinhold vols.1-2., 1st Edition, 998 pages; 3rd edn. Minuteman Press, 2010; vols. 2-3, fifth edition (in press)
↑Magde D.; Elson E. L.; Webb W. W. (1972). "Thermodynamic fluctuations in a reacting system: Measurement by fluorescence correlation spectroscopy, (1972)". Phys Rev Lett29 (11): 705–708. doi:10.1103/physrevlett.29.705.
↑Elson E. L., Magde D. (1974). "Fluorescence correlation spectroscopy I. Conceptual basis and theory, (1974)". Biopolymers13: 1–27. doi:10.1002/bip.1974.360130102.
↑Magde D.; Elson E. L.; Webb W. W. (1974). "Fluorescence correlation spectroscopy II. An experimental realization, (1974)". Biopolymers13 (1): 29–61. doi:10.1002/bip.1974.360130103. PMID4818131.
↑Thompson N L 1991 Topics in Fluorescence Spectroscopy Techniques vol 1, ed J R Lakowicz (New York: Plenum) pp 337–78
↑Gohlke, R. S. (1959). "Time-of-Flight Mass Spectrometry and Gas-Liquid Partition Chromatography". Analytical Chemistry31 (4): 535–541. doi:10.1021/ac50164a024.
↑Gohlke, R; McLafferty, Fred W. (1993). "Early gas chromatography/mass spectrometry". Journal of the American Society for Mass Spectrometry4 (5): 367–71. doi:10.1016/1044-0305(93)85001-E. PMID24234933.