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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]
In the less extensive technique of equilibrium unfolding, the fractions of folded and unfolded molecules (denoted as and , respectively) are measured as the solution conditions are gradually changed from those favoring the native state to those favoring the unfolded state, e.g., by adding a denaturant such as guanidinium hydrochloride or urea.
They can also be converted into glucose. [4] This glucose can then be converted to triglycerides and stored in fat cells. [5] Proteins can be broken down by enzymes known as peptidases or can break down as a result of denaturation. Proteins can denature in environmental conditions the protein is not made for. [6]
The gelatinization temperature of starch depends upon plant type and the amount of water present, pH, types and concentration of salt, sugar, fat and protein in the recipe, as well as starch derivatisation technology are used. Some types of unmodified native starches start swelling at 55 °C, other types at 85 °C. [3]
Table sugar (sucrose) is converted to invert sugar by hydrolysis. Heating a mixture or solution of table sugar and water breaks the chemical bond that links together the two simple-sugar components. The balanced chemical equation for the hydrolysis of sucrose into glucose and fructose is:
Calcium caseinate is generally stable at a pH above 5.7, and appears as a milky liquid. This is unlike ammonium, potassium, and sodium caseinates , which are practically clear. At a neutral or acidic pH, casein is relatively insoluble in water, and is easily separated from other milk proteins, sugars, and minerals.
In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to a protein or lipid. [1] Glycosylation occurs at defined sites on the target molecule. It is a common form of post-translational modification of proteins and is required for the functioning of the mature protein.
The basic proteoglycan unit consists of a "core protein" with one or more covalently attached glycosaminoglycan (GAG) chain(s). [2] The point of attachment is a serine (Ser) residue to which the glycosaminoglycan is joined through a tetrasaccharide bridge (e.g. chondroitin sulfate - GlcA - Gal -Gal- Xyl -PROTEIN).