Book Synopsis Enzyme-induced Gelation of Whey Proteins by :
Download or read book Enzyme-induced Gelation of Whey Proteins written by and published by . This book was released on 2003 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: There is currently an array of whey protein hydrolysates on the market. The applications for these products include but are not limited to: improved heat stability; reduced allergenicity; production of bioactive peptides; tailoring amounts and size of peptides for special diets; and altering the functional properties of gelation, foaming and emulsification. With functional properties applications, hydrolyzed proteins offer advantages over unmodified proteins in increased solubility, heat-process stability, foaming and emulsification. Customers who are buying whey protein hydrolysates for nutritional applications (sports nutrition, enteral formulas, hypoallergenic infant formulae, etc.) are looking for products with a high degree of hydrolysis (generally>10%) and a high content in short peptides. Extensive enzymatic hydrolysis is required, preferentially with an endoprotease, in order to avoid the presence of free amino acids in the final product. However, some endoproteases (e.g. Alcalase 2.4L) produce peptides that aggregate and form a gel during the course of hydrolysis. This creates a hurdle when a high degree of hydrolysis is desired. Because the array of endoproteases commercially available is not very exhaustive, and some enzymes and hydrolysis conditions cause gelation problems, it is important to understand the gelation mechanism in order to solve it and ultimately produce hydrolysates with a high degree of hydrolysis. The first objective of this study was to compare enzyme-induced gelation of extensively hydrolyzed whey proteins by Alcalase with the plastein reaction by determining the types of interactions. The average chain length of the peptides did not increase during hydrolysis and reached a plateau after 30 min to be about 4 residues, suggesting that the gel was formed by small molecular weight peptides held together by non-covalent interactions. The enzyme-induced gel network was stable over a wide range of pH and ionic strength, and therefore showe.