Genetic Engineering of Milk Proteins and Proteases

One of the most important factors that determine whether or not a protein is usable in the fabrication of a food product is its functionality. The functionality results from a combination of physico-chemical properties that define the behavior of the food protein in food systems. It is evident that a detailed understanding of food protein functionality requires an intimate knowledge of the protein structure. The bovine milk protein system has been studied in great detail. Although providing useful structure-function 

Recent developments in recombinant DNA technology can be used to systematically alter single amino acids in the primary sequence of proteins. It is known that single changes in amino acids can markedly alter the functional characteristics of proteins. 

The events leading to the macromolecular associations observed with (3-lactoglobulin appear to be mediated by disulfide interactions. The initial solution proposed to reduce thermoinduced aggregation was to remove the Cys 121 and replace it with alanine (Cho et al., 1994). Unfortunately, recombinant protein could not be purified from inclusion bodies. The alternative 

The key issue with a number of modifications that have been made to (3-lactoglobulin is their performance as food ingredients, especially when added to complex formulations (Lee et al., 1994). As a model system, yoghurt is simple and could be improved by reducing whey syneresis. Since the double 

DESIGN OF RECOMBINANT ENZYMES USED FOR PROTEIN MODIFICATION 

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E. Liberation of Biologically Functional Peptides IV Genetic Engineering of Milk Proteins and Proteases... 

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