Texturization ionic strengths

Although less frequently discussed, heat processes often influence the textures and chemistries of the intermediate and end products, and thermal treatments are not without consequences on milk proteins that are denatured. Denaturation of proteins occurs under precise conditions of pH, temperature and ionic strength leading to their unfolding. Denaturation is significantly slower when proteins are near their isoelectric point. Only (3-lactoglobulin is irreversibly denatured at pH 7 and 70°C a-lactalbumin is denatured at pH 6.7 and 65°C. Aggregation of these proteins, besides hydrophobic... 

The variety of mechanisms that may be involved in the sorption process of metal ions onto activated carbon induces a great number of factors that control the adsorption the surface oxygen complex content, the pH of point of zero charge, the pore texture of carbon, the solution pH and its ionic strength, the adsorption temperature, the nature of the metal ion given by its speciation diagram, its solubility, and its size in adsorption conditions. The influence of these various conditions is detailed in Section 24.2.1.4. 

Among the characteristics of the adsorbent are its pore texture, surface chemistry, and mineral matter content. The characteristics of the adsorptive are its molecular size, solubility, polarity, pIC, (for electrolytes), and nature of the substituents if it is aromatic. Finally, the solution chemistry factors are the pH and the ionic strength [5]. I shall focus in this section only on the role of the characteristics of the adsorbent, especially its carbon surface chemistry, on the adsorption processes, because although its importance has long been recognized [6, 7], the exact nature of this importance has often been controversial and misunderstood [1]. 

Additive Concentration (moll1) Ionic strength Disintegration time (min) CP <°C) Matrix texture ... 

Basically, there are three major groups of proteins in muscle tissue (a) the sarcoplasmic proteins of the muscle cell cytoplasm, (b) the myofibrillar proteins, soluble at high ionic strengths, that make up the myofibril or contractile part of the muscle, and (c) the stromal proteins comprised largely of the connective tissue proteins, collagen, and elastin. The myofibrillar proteins and the stromal proteins are fibrous and elongated they form viscous solutions with large shear resistance. These properties coupled with other lines of indirect evidence indicate that the physical properties of the myofibrillar and stromal proteins are directly related to the texture and tenderness of meat (34). 

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