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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]
Egg white consists primarily of about 90% water into which about 10% proteins (including albumins, mucoproteins, and globulins) are dissolved. 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 ...
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.
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.
The immunoglobulin superfamily (IgSF) is a large protein superfamily of cell surface and soluble proteins that are involved in the recognition, binding, or adhesion processes of cells.
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.
Whether you’ve got a can of bacon grease at the ready or you’re Team Butter, we won’t be swearing off the fats when we’re cooking around here.