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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, 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.
The crusts of most breads, such as this brioche, are golden-brown mostly as a result of the Maillard reaction.. The Maillard reaction (/ m aɪ ˈ j ɑːr / my-YAR; French:) is a chemical reaction between amino acids and reducing sugars to create melanoidins, the compounds that give browned food its distinctive flavor.
Deamination is the removal of an amino group from a molecule. [1] Enzymes that catalyse this reaction are called deaminases. In the human body, deamination takes place primarily in the liver; however, it can also occur in the kidney. In situations of excess protein intake, deamination is used to break down amino acids for energy.
Food physical chemistry is considered to be a branch of Food chemistry [1] [2] concerned with the study of both physical and chemical interactions in foods in terms of physical and chemical principles applied to food systems, as well as the applications of physical/chemical techniques and instrumentation for the study of foods.
Primary nutritional groups are groups of organisms, divided in relation to the nutrition mode according to the sources of energy and carbon, needed for living, growth and reproduction. The sources of energy can be light or chemical compounds; the sources of carbon can be of organic or inorganic origin.
For example, extremes of pH or temperature usually cause denaturation of all protein structure, but this is a non-specific effect. Similarly, some non-specific chemical treatments destroy protein structure: for example, heating in concentrated hydrochloric acid will hydrolyse the peptide bonds holding proteins together, releasing free amino acids.
For example, in the UK the third edition of The Composition of Foods [3] presented data on vitamin content of foods. However, due to the amount of information already available and in order to avoid the need to analyse every food for every vitamin, values from the scientific literature were included, although the tables are still predominately ...