Enzyme and Chemical Modification of Proteins

• Published in: Food Proteins and Their Applications pp. 393 - 423
• Main Author: Schwenke, Klaus Dieter
• Format: Book Chapter
• Language: English
• Published: United Kingdom Routledge 1997; Taylor & Francis Group
• Edition: 1
• Subjects: Food & beverage technology; Faba Bean; 11S Globulins; Protein Hydrolysates; Soy Protein Isolate; Soy Protein; Amino Acid Ester; Molecular Weight Glutenin Subunits; Proteolytic Modification; SPI; Pea Legumin; Plastein Reaction; cAMP Dependent Kinase; Food Proteins; Protein Isolate; Soybean Glycinin; Citraconic Anhydride; Soybean Protein; Native Casein; Surface Functional Properties; Deamidation Level; EA; FC; Succinylated Proteins
• DOI: 10.1201/9780203755617-13
• ISBN: 9780824798208; 0824798201

This chapter focuses on relevant methods of food protein modification with regard to functional properties and nutritional implications. Only representative examples are selected from the enormous number of published papers on chemical and enzymatic modification of food proteins. Food proteins in their natural state do not necessarily possess optimal nutritional and functional properties. Egg proteins are boiled so as to increase their digestibility. Meat is cooked or roasted so as to make it more palatable and also to improve both its nutritive and its organoleptic properties. A large number of papers describe the effect of proteolytic breakdown of food proteins on their functional properties. They comprise animal proteins such as casein, soybean proteins, faba bean proteins, wheat gluten and gluten fractions, maize proteins, oat flour, cottonseed proteins, sunflower, and rapeseed proteins, among others. Proteolytic modification has special importance for the improvement of solubility of proteins, e.g., from cereals that are poorly soluble in aqueous media.