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  2. Denaturation (biochemistry) - Wikipedia

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

    The effects of temperature on enzyme activity. Top: increasing temperature increases the rate of reaction (Q10 coefficient). Middle: the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom: consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  3. Q10 (temperature coefficient) - Wikipedia

    en.wikipedia.org/wiki/Q10_(temperature_coefficient)

    The effects of temperature on enzyme activity. Top - increasing temperature increases the rate of reaction (Q 10 coefficient). Middle - the fraction of folded and functional enzyme decreases above its denaturation temperature. Bottom - consequently, an enzyme's optimal rate of reaction is at an intermediate temperature.

  4. Catalase - Wikipedia

    en.wikipedia.org/wiki/Catalase

    Catalase has one of the highest turnover numbers of all enzymes; one catalase molecule can convert millions of hydrogen peroxide molecules to water and oxygen each second. [ 6 ] Catalase is a tetramer of four polypeptide chains, each over 500 amino acids long. [ 7 ]

  5. Chlorophyllase - Wikipedia

    en.wikipedia.org/wiki/Chlorophyllase

    The activity of chlorophyllase also depends on the pH and ionic content of the medium. The values of kcat and kcat/Km of chlorophyllase in the presence of chlorophyll showed pKa values of 6.3 and 6.7, respectively. Temperature also affects chlorophyllase activity. Wheat chlorophyllase is active from 25 to 75 °C.

  6. Amylase - Wikipedia

    en.wikipedia.org/wiki/Amylase

    Different temperatures optimize the activity of alpha or beta amylase, resulting in different mixtures of fermentable and unfermentable sugars. In selecting mash temperature and grain-to-water ratio, a brewer can change the alcohol content, mouthfeel , aroma, and flavor of the finished beer.

  7. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    Enzyme activity initially increases with temperature (Q10 coefficient) until the enzyme's structure unfolds (denaturation), leading to an optimal rate of reaction at an intermediate temperature. See also: Protein structure

  8. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Protein backbones are very stable in water at neutral pH and room temperature, although the rate of hydrolysis of different peptide bonds can vary. The half life of a peptide bond under normal conditions can range from 7 years to 350 years, even higher for peptides protected by modified terminus or within the protein interior.

  9. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    Enzyme activity as given in katal generally refers to that of the assumed natural target substrate of the enzyme. Enzyme activity can also be given as that of certain standardized substrates, such as gelatin, then measured in gelatin digesting units (GDU), or milk proteins, then measured in milk clotting units (MCU). The units GDU and MCU are ...