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The casein polymerization
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The rennet casein used in the polymerization process is a heap of macromolecular chains composed, seemingly, of all the existing types of casein (αS1 ,αS2 ,β and κ) since no purification is carried out prior to implementation. The interactions between the chains are mainly physical with Vander Waals - type links and especially hydrogen links.

When implementing, there are several combined actions to be taken into consideration during polymerization.

First of all, the joint action of temperature and pressure that, firstly, denatures, even hydrolyzes, the native casein protein and, secondly, increases the mobility of the chains of recycled (poly)casein. These severe conditions allow the dioxygen to attack the cystein's thiolic functions so as to form disulfide links through an oxidation-reduction reaction. The disulfide bridges can be formed from two cystein units in the same polypeptide chain (formation of a loop) or from two different chains (formation of a three-dimensional array). The chemical bridge is quite different from that of the native protein as high-energy covalent links are involved.

The glycerol and ethanol produce an esterification reaction between these alcohols and the carboxylic groups. The esters formed preferentially on the lateral chains increase considerably the proportion of hydrogen links possible between the casein chains. With respect to the native protein (non-esterified protein), the proportion of physical bridging is clearly increased. The alcohols and water also swell up and plasticize the (poly)casein array already formed in the recycled product. This allows the unreticulated casein to diffuse into the array.

The casein polymerizes and can then be worked like plastic.

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