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Hen egg white lysozyme is thermally stable, with a melting point reaching up to 72 °C at pH 5.0. [5] However, lysozyme in human milk loses activity very quickly at that temperature. [6] Hen egg white lysozyme maintains its activity in a large range of pH (6–9). [7] Its isoelectric point is 11.35. [8]
Unlike the yolk, which is high in lipids (fats), egg white contains almost no fat, and carbohydrate content is less than 1%. Egg whites contain about 56% of the protein in the egg. Egg white has many uses in food (e.g. meringue, mousse) as well as many other uses (e.g. in the preparation of vaccines such as those for influenza [2]).
The mechanism is illustrated below for hen egg white lysozyme. [ 15 ] An alternative mechanism for hydrolysis with retention of stereochemistry can occur that proceeds through a nucleophilic residue that is bound to the substrate, rather than being attached to the enzyme.
Eggs play a big role in many people's protein intake, but you might wonder exactly how much is it packing. Ahead, experts break down all the benefits of the food.
Lysozyme type C and alpha-lactalbumin are similar both in terms of primary sequence and structure, and probably evolved from a common ancestral protein. [12] Around 35 to 40% of the residues are conserved in both proteins as well as the positions of the four disulphide bonds. There is, however, no similarity in function.
In molecular biology, glycoside hydrolase family 24 is a family of glycoside hydrolases. Glycoside hydrolases EC 3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety.
Many species of bacteria are subject to lysis by the enzyme lysozyme, found in animal saliva, egg white, and other secretions. [1] Phage lytic enzymes produced during bacteriophage infection are responsible for the ability of these viruses to lyse bacterial cells. [2]
This protein provides essential amino acids and bioactive compounds necessary for optimal growth, development, and health. α-Lactalbumin is the most abundant whey protein in human milk and its properties have been researched to include in infant formulas to replicate mammary milk compounds. This protein is a strong source of branched amino ...