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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]
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.
Denaturation (biochemistry), a structural change in macromolecules caused by extreme conditions; Denaturation (fissile materials), transforming fissile materials so that they cannot be used in nuclear weapons; Denaturation (food), intentional adulteration of food or drink rendering it unfit for consumption while remaining suitable for other uses
A specially denatured alcohol (SDA) is one of many types of denatured alcohol specified under the United States Title 27 of the Code of Federal Regulations Section 21.151. [11] A specially denatured alcohol is a combination of ethanol and another chemical substance, e.g., ethyl acetate in SDA 29, 35, and 35A , added to render the mixture ...
For example, collagen, found in connective tissue, bones, and cartilage, and keratin, found in nails, claws, and hair, have observed stiffnesses that are several orders of magnitude higher than that of elastin, [104] which is though to give elasticity to structures such as blood vessels, pulmonary tissue, and bladder tissue, among others.
Examples of sources of gluten (clockwise from top): wheat as flour, spelt, barley, and rye as rolled flakes Gluten is a structural protein naturally found in certain cereal grains . [ 1 ] The term gluten usually refers to the elastic network of a wheat grain's proteins, gliadin and glutenin primarily, that forms readily with the addition of ...
In molecular biology, molecular chaperones are proteins that assist the conformational folding or unfolding of large proteins or macromolecular protein complexes. There are a number of classes of molecular chaperones, all of which function to assist large proteins in proper protein folding during or after synthesis, and after partial denaturation.
For example, spray drying after membrane filtration separates the proteins from whey. [8] Heat denatures whey proteins, causing them to coagulate into a protein gel that may be useful in some foods. Sustained high temperatures above 72 °C can denature whey proteins. [7] Heat-denatured whey can still cause allergies in some people. [9]