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amylose is the linear fraction of starch. Commercial samples of amylose usually occur<br />

in retrograded, water insoluble form, which can be solubillized by pressure cooking at<br />

150-160 o C. On cooling, amylose solutions of 2% or higher concentrations, prepared<br />

in this way, rapidly gel, while at concentrations lower than 2% precipitation occurs<br />

(Schoch, 1964). Amylose is also soluble in dilute alkali, and rapid neutralization of<br />

concentrations greater than 2% results in gel formation. Both the gelation of amylose<br />

from concentrated solutions and precipitation from dilute solution can be termed<br />

retrogradation. The gels and precipitates formed result from the inherent tendency of<br />

amylose molecules to undergo conformational ordering and to tendency of amylose<br />

molecules to undergo conformation ordering and to subsequently align or aggregate<br />

(Gidley and Bulpin, 1989). The rate of retrogradation increases with increasing<br />

amylose concentration and with decreasing temperature and is greatest at pH 5-7. In<br />

addition, the retrogradation rate has a sharp maximum at amylose degree of<br />

polymerization (DP) of 80, shorter and longer molecules being much more soluble<br />

(Ring et al. 1987 and Jacobson et al. 1997).<br />

Goodfellow and Wilson (1990) studied the retrogradation of<br />

amylose using Fourier Transform Infrared (FT-IR). They found that helix formation<br />

must occur before the creation of crystallites; therefore double helix must form at the<br />

short or early on in the gelation process. Thus in summary, a same time as phase<br />

separation, to create a gel network, with subsequent aggregation of these helices<br />

producing crystallinity would be consistent with the experimental data (Figure 9). The<br />

IR results for amylopectin suggest an initial fast change followed by a much slow<br />

change. Previous IR work by Wilson et al. (1987) in which the spectra for<br />

amylopectin from 6 to 340 hour were obtained suggest that FT-IR and G´ monitor the<br />

same process-namely the crystallization of the amylopectin side chains followed by a<br />

slow aggregation of these helices to produce crystallinity (Figure 9) .<br />

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