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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. Alliinase - Wikipedia

    en.wikipedia.org/wiki/Alliinase

    These enzymes are found in plants of the genus Allium, such as garlic and onions. Alliinase is responsible for catalyzing chemical reactions that produce the volatile chemicals that give these foods their flavors, odors, and tear-inducing properties. Alliinases are part of the plant's defense against herbivores.

  4. Pectinase - Wikipedia

    en.wikipedia.org/wiki/Pectinase

    Pectinase enzymes used today are naturally produced by fungi and yeasts (50%), insects, bacteria and microbes (35%) and various plants (15%), [4] but cannot be synthesized by animal or human cells. [5] In plants, pectinase enzymes hydrolyze pectin that is found in the cell wall, allowing for new growth and changes to be made.

  5. Q10 (temperature coefficient) - Wikipedia

    en.wikipedia.org/wiki/Q10_(temperature_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. The temperature of a muscle has a significant effect on the velocity and power of the muscle contraction, with performance generally declining with ...

  6. Catechol oxidase - Wikipedia

    en.wikipedia.org/wiki/Catechol_oxidase

    In plants, both enzymes can catalyze the oxidation of ortho-diphenols substrates into their corresponding ortho-quinones. The key difference between the two related enzymes is that tyrosinase can catalyze the hydroxylation of monophenols to diphenols (monophenolase activity) as well as the oxidation of the o-diphenol to the o-quinone ...

  7. Myrosinase - Wikipedia

    en.wikipedia.org/wiki/Myrosinase

    Ascorbate is a known cofactor of myrosinase, serving as a base catalyst in glucosinolate hydrolysis. [1] [7] For example, myrosinase isolated from daikon (Raphanus sativus) demonstrated an increase in V max from 2.06 μmol/min per mg of protein to 280 μmol/min per mg of protein on the substrate, allyl glucosinolate (sinigrin) when in the presence of 500 μM ascorbate. [4]

  8. Polyphenol oxidase - Wikipedia

    en.wikipedia.org/wiki/Polyphenol_oxidase

    Polyphenol oxidase is an enzyme found throughout the plant and animal kingdoms, [31] including most fruits and vegetables. [32] PPO has importance to the food industry because it catalyzes enzymatic browning when tissue is damaged from bruising, compression or indentations, making the produce less marketable and causing economic loss.

  9. Heat shock response - Wikipedia

    en.wikipedia.org/wiki/Heat_shock_response

    The heat shock response (HSR) is a cell stress response that increases the number of molecular chaperones to combat the negative effects on proteins caused by stressors such as increased temperatures, oxidative stress, and heavy metals. [1]