Amino hydration capacity

Functionality factors include water absorption/hydration capacity, fat absorption, cooking time, protein functionality (amino acid and protein subunit composition), and starch functionality, which is associated with the amylose-to-amylopectin ratio. The amylose-to-amylopectin ratio affects the texture of cooked products. The texture of foods prepared from varieties with low amylose content tends to be stiffer than that of foods cooked from varieties with high amylose content. 

The protein that stores iron in the body is called ferritin. A ferritin molecule consists of a protein coat and an iron-containing core. The outer coat is made up of 24 pol3q5eptide chains, each with about 175 amino acids. As Figure 20-27 shows, the pol q5eptides pack together to form a sphere. The sphere is hollow, and channels through the protein coat allow movement of iron in and out of the molecule. The core of the protein contains hydrated iron(HI) oxide, FC2 O3 H2 O. The protein retains its shape whether or not iron is stored on the inside. When filled to capacity, one ferritin molecule holds as many as 4500 iron atoms, but the core is only partially filled under normal conditions. In this way, the protein has the capacity to provide iron as needed for hemoglobin s mthesis or to store iron if an excess is absorbed by the body. 

Makhatadze GI, Privalov PL. Heat capacity of proteins. I. Partial 33. molar heat capacity of individual amino acid residues in aqueous solution hydration effect. J. Mol. Biol. 1990 213 375-384. 

Tables 8.2 and 8.3 present molar heat capacities of solid amino acids and polyamino acids. Table 8.4 presents specific heat capacities of anhydrous and hydrated proteins. All of the measurements were done by using adiabatic absolute calorimetry and their accuracy is better than 1-2%. Heat capacity of anhydrous proteins can be predicted using empirical approach developed by Wunderlich (see e.g., [1]).

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