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  2. Denaturation (biochemistry) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(biochemistry)

    In biochemistry, denaturation is a process in which proteins or nucleic acids lose folded structure present in their native state due to various factors, including application of some external stress or compound, such as a strong acid or base, a concentrated inorganic salt, an organic solvent (e.g., alcohol or chloroform), agitation and radiation, or heat. [3]

  3. Pasteurization - Wikipedia

    en.wikipedia.org/wiki/Pasteurization

    Pasteurized milk in Japan A 1912 Chicago Department of Health poster explains household pasteurization to mothers.. In food processing, pasteurization (also pasteurisation) is a process of food preservation in which packaged and unpacked [clarification needed] foods (e.g., milk and fruit juices) are treated with mild heat, usually to less than 100 °C (212 °F), to eliminate pathogens and ...

  4. Denaturation (food) - Wikipedia

    en.wikipedia.org/wiki/Denaturation_(food)

    Denaturation is the process by which or foods or liquids are made unpleasant or dangerous to consume; it is done by adding a substance known as a denaturant. Aversive agents —primarily bitterants and pungent agents —are often used to produce an unpleasant flavor. For example, the bitterant denatonium might be added to food used in a ...

  5. Pepsin - Wikipedia

    en.wikipedia.org/wiki/Pepsin

    Pepsin / ˈpɛpsɪn / is an endopeptidase that breaks down proteins into smaller peptides and amino acids. It is one of the main digestive enzymes in the digestive systems of humans and many other animals, where it helps digest the proteins in food. Pepsin is an aspartic protease, using a catalytic aspartate in its active site.

  6. Casein - Wikipedia

    en.wikipedia.org/wiki/Casein

    Casein. Casein (/ ˈkeɪsiːn / KAY-seen, from Latin caseus "cheese") is a family of related phosphoproteins (αS1, aS2, β, κ) that are commonly found in mammalian milk, comprising about 80% of the proteins in cow's milk and between 20% and 60% of the proteins in human milk. [1] Sheep and cow milk have a higher casein content than other types ...

  7. Globular protein - Wikipedia

    en.wikipedia.org/wiki/Globular_protein

    Globular proteins are somewhat water-soluble (forming colloids in water), unlike the fibrous or membrane proteins. [1] There are multiple fold classes of globular proteins, since there are many different architectures that can fold into a roughly spherical shape. The term globin can refer more specifically to proteins including the globin fold.

  8. Food physical chemistry - Wikipedia

    en.wikipedia.org/wiki/Food_physical_chemistry

    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 ...

  9. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    Polyphenol oxidase (PPO; also polyphenol oxidase i, chloroplastic), an enzyme involved in fruit browning, is a tetramer that contains four atoms of copper per molecule. [1] PPO may accept monophenols and/or o -diphenols as substrates. [2]