Casein modified, functional properties

Chemical derivatization of proteins to modify functional properties has received limited consideration. Cationic derivatives of food proteins are routinely used (e.g. sodium soy isolates and sodium and calcium caseinates) to improve wettability, dispersibility and handling properties of these proteins (27). 

If this latter function could be accomplished, it would probably permit the development of new caseinate forms with modified functional properties. 

Some physical and functional properties of casein modified by the covalent attachment of amino acids are given in Table IX. Despite extensive modification, the relative viscosities of 2% solutions of the modified proteins did not change significantly, with the exception of aspartyl casein which was more viscous. There was some decrease in the solubilities of aspartyl casein and tryptophyl casein as compared with the casein control. It is anticipated that adding some 11.4 tryptophyl residues per mole of casein would decrease the aqueous solubility of the modified protein. However the results with aspartyl casein are unexpected. The changes in viscosity, solubility, and fluorescence indicate that aspartyl casein is likely to be a more extended molecule than the casein control. There was a marked decrease in the fluorescence of aspartyl casein and tryptophyl casein (see Table IX). The ratios of the fluorescences of acetylmethionyl casein to methionyl casein and t-BOC-tryptophyl casein to tryptophan casein were 1.20 and 2.01, respectively, indicating the major effects that these acyl groups have on the structure of the casein. 

Canton, M., Mulvihill, D.M. 1982. Functional properties of commercial and chemically modified caseins and caseinates. Irish J. Food Sci. Technol. 6, 107 (abstract). 

There have been a limited number of studies on the effects of enzymic modification of protein concentrates on functional properties other than solubility. Studies on functional properties, as modified by enzymic treatments, emphasize foam formation and emulsifying characteristics of the hydrolysates. Treatment of chicken egg albumen alters the functional properties of the egg proteins in terms of foam volume and stability and the behavior of the proteins in angel food cakes (25). Various proteolytic enzymes were used to degrade the egg albumen partially. However, proteolytic enzyme inhibitors indigenous to the egg proteins repressed hydrolysis of the egg proteins compared with casein. 

Functional properties of some enzymatically modified and EPM-treated products of milk proteins [136] were determined as follows. An enzymatically prehydrolyzed commercial milk protein concentrate (SR) without further hydrolysis, and casein hydrolyzed by alcalase, a-chymotrypsin, and papain, respectively, were used as substrates in the EPM reaction. The concentration of the hydrolysates was 20% w/ v in the EPM reactions. A methionine methyl ester hydrochloride/ substrate ratio of 1 5 was used for incorporating this amino acid. After incubation, the products with methionine incorporation were simultaneously dialyzed for 2 days through a cellophane membrane against distilled water. The nondialyzable fractions and the EPM products without amino acid enrichment were freeze-dried. Covalent methionine incorporation in the EPM products with amino acid enrichment was verified by exopeptidase hydrolysis of the protein chains. The functional properties of the different EPM products are summarized in Table 1. An important functional property of proteins and/or peptide mixtures is their emulsifying behavior. This is highly influenced by the molecular structure, the position and ratio of hydrophobic-hydrophilic amino acids. Emulsion activity was found to be low (34.0) for casein, and the values determined for enzyme hydrolyzed and modified products were in general even lower. The papain hydrolysate, sample H3, showed here a different behavior as well this was the one of the sample series that had the highest EAI value (43.0). The emulsion stability of the enzymatically modified products displayed tendencies quite opposite to the values of emul-... 

Table 1 Functional Properties of Casein and Enzymatically Modified Proteinsab...

Raw milk is a unique agricultural commodity. It contains emulsified globular lipids and colloidally dispersed proteins that may be easily modified, concentrated, or separated in relatively pure form from lactose and various salts that are in true solution. With these physical-chemical properties, an array of milk products and dairy-derived functional food ingredients has been developed and manufactured. Some, like cheese, butter, and certain fermented dairy foods, were developed in antiquity. Other dairy foods, like nonfat dry milk, ice cream, casein, and whey derivatives, are relatively recent products of science and technology. This chapter describes and explains the composition of traditional milk products, as well as that of some of the more recently developed or modified milk products designed to be competitive in the modern food industry. 

More details of the chemical modification of casein and other food proteins with carboxyl-amino acid anhydrides will be published elsewhere. Depending on the distribution and length of copolymers of methionine covalently linked to proteins, distinct effects on functional and nutritional properties of the modified proteins are expected. 

The BT/KPVS complex is not soluble over a wide range of pH It also exhibits considerable enzymatic activities towards BAN A and casein (Figs. 18.9 and 18.11). Thus, the complex can be expected to function as an immobilized enzyme. However, several difficulties arise in handling the complexed enzyme, because it is in the form of an amorphous precipitate. It seems desirable to modify its morphological properties through an appropriate method such as gel entrapment. 

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