Thorn Huppertz

Disruption and reassociation of casein micelles under high pressure.

High pressure (HP) treatment affects many constituents of milk (for reviews see Huppertz et al. 2002; Needs, 2002); particular in the properties of casein micelles in HP-treated milk differ considerably from their counterparts in untreated milk. In milk treated at 100–200 MPa, average casein micelle size differs little from that of untreated milk (Needs et al. 2000a; Huppertz et al. 2004a; Regnault et al. 2004; Anema et al. 2005), but micelle size in milk treated at 250 MPa for [ges ]15 min is considerably higher than in untreated milk, probably due to HP-induced aggregation of casein micelles (Huppertz et al. 2004a,b; Regnault et al. 2004); after treatment at 300–800 MPa, micelle size is ~50% lower than that in untreated milk (Needs et al. 2000a; Huppertz et al. 2004a,b; Anema et al. 2005). HP-induced changes in average casein micelle size are irreversible on subsequent storage, except for the increase in micelle size after treatment at 250 MPa (Huppertz et al. 2004a).

Physical Chemistry of Milk Fat Globules

Whole milk or cream can be regarded as an emulsion of milk fat globules in milk plasma. The physico-chemical properties of the milk fat globules affect many properties of liquid dairy products such as milk and cream, and as such should always be considered when studying the stability of liquid dairy products. The physicochemical properties of the milk fat globules can be influenced through a wide variety of processes, as described in this chapter and, once chosen and controlled carefully, these processes can be efficiently used to give products desired characteristics (e.g., in terms of storage stability or rheological properties). Although much is known concerning physico-chemical properties of the milk fat globules, and instability of dairy emulsions can be controlled well with the current state of knowledge, gathering further information concerning the physical chemistry of milk fat globules, and the underlying fundamental problems, remains crucial. Pursuit of fundamental knowledge often leads to good results, sometimes in unexpected ways. Thus, it is important to continue to enhance our understanding of areas such as those described in this chapter.

Reformation of casein particles from alkaline-disrupted casein micelles

In this study, the properties of casein particles reformed from alkaline disrupted casein micelles were studied. For this purpose, micelles were disrupted completely by increasing milk pH to 10.0, and subsequently reformed by decreasing milk pH to 6.6. Reformed casein particles were smaller than native micelles and had a slightly lower zeta-potential. Levels of ionic and serum calcium, as well as rennet coagulation time did not differ between milk containing native micelles or reformed casein particles. Ethanol stability and heat stability, >pH 7.0, were lower for reformed casein particles than native micelles. Differences in heat stability, ethanol stability and zeta-potential can be explained in terms of the influence of increased concentrations of sodium and chloride ions in milk containing reformed casein particles. Hence, these results indicate that, if performed in a controlled manner, casein particles with properties closely similar to those of native micelles can be reformed from alkaline disrupted casein micelles.

Influence of ethanol on the rennet-induced coagulation of milk.

The influence of ethanol on the rennet-induced coagulation of milk was studied to investigate potential synergistic effects of these two mechanisms of destabilisation on the casein micelles. Addition of 5% (v/v) ethanol reduced the rennet coagulation time (RCT) of milk, whereas higher levels of ethanol (10-20%, v/v) progressively increased RCT. The temperature at which milk was coagulable by rennet decreased with increasing ethanol content of the milk. The primary stage of rennet coagulation, i.e., the enzymatic hydrolysis of kappa-casein, was progressively slowed with increasing ethanol content (5-20%, v/v), possibly due to ethanol-induced conformational changes in the enzyme molecule. The secondary stage of rennet coagulation, i.e., the aggregation of kappa-casein-depleted micelles, was enhanced in the presence of 5-15% ethanol, the effect being largest at 5% ethanol. Enhanced aggregation of micelles is probably due to an ethanol-induced decrease in inter-micellar steric repulsion. These results indicate an interrelationship between the effects of ethanol and chymosin on the casein micelles in milk, which may have interesting implications for properties of dairy products.