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  2. 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.

  3. 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.

  4. Enzyme assay - Wikipedia

    en.wikipedia.org/wiki/Enzyme_assay

    5.2 Effects of Temperature. 5.3 Effects of pH. 5.4 Enzyme ... Enzyme activity is a measure of the quantity of active enzyme present and is thus dependent on various ...

  5. Enzyme - Wikipedia

    en.wikipedia.org/wiki/Enzyme

    An enzyme's activity decreases markedly outside its optimal temperature and pH, and many enzymes ... Enzyme activity. ... affect each other. The enzyme's function is ...

  6. Papain - Wikipedia

    en.wikipedia.org/wiki/Papain

    The enzyme is deacylated by a water molecule and releases the carboxy terminal portion of the peptide. In immunology, papain is known to cleave the Fc (crystallisable) portion of immunoglobulins (antibodies) from the Fab (antigen-binding) portion. Papain is a relatively heat-resistant enzyme, with an optimal temperature range of 60 to 70 °C. [9]

  7. Michaelis–Menten kinetics - Wikipedia

    en.wikipedia.org/wiki/Michaelis–Menten_kinetics

    A decade before Michaelis and Menten, Victor Henri found that enzyme reactions could be explained by assuming a binding interaction between the enzyme and the substrate. [11] His work was taken up by Michaelis and Menten, who investigated the kinetics of invertase, an enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose. [12]

  8. Enzyme kinetics - Wikipedia

    en.wikipedia.org/wiki/Enzyme_kinetics

    Enzyme inhibitors are molecules that reduce or abolish enzyme activity, while enzyme activators are molecules that increase the catalytic rate of enzymes. These interactions can be either reversible (i.e., removal of the inhibitor restores enzyme activity) or irreversible (i.e., the inhibitor permanently inactivates the enzyme).

  9. Bromelain - Wikipedia

    en.wikipedia.org/wiki/Bromelain

    After an hour at 50 °C (122 °F), 83% of the enzyme remains, while at 40 °C (104 °F), practically 100% remains. [6] The proteolytic activity of concentrated bromelain solutions remains relatively stable for at least 1 week at room temperature, and multiple freeze-thaw cycles or exposure to the digestive enzyme trypsin have little effect on it.