Explain functional properties of protein hydrolysis

Hydrolysis of food proteins using proteases (trypsin, chymootrypsin, papain and thermolysin) alters their functional properties.  Extensive hydrolysis by nonspecific proteases, such as papain, cause stabilization of even poorly soluble proteins. Such hydrolysates usually contain low molecular weight epties of the order 2-4 amino acids residues. Extensive hydrolysis damages several functional properties, such as gelation, foaming and emulsifying properties. These modified proteins are useful in  liquid-type foods, such as soups and sauces, where solubility is a primary criterion and feeding a person who might not be able to digest solid foods.

Partial hydrolysis of  proteins either by using site-specific enzymes (such as trypsin or chymotrypsin) or by control of hydrolysis time, often improves foaming and emulsification properties, but not gelling properties. With some proteins, partial hydrolysis may cause a transient decrease in solubility, because of exposure of the buried hydrophobic regions.