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Annual Progress Report on Malting Barley Research March, 2007

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M w kDa<br />

800<br />

600<br />

400<br />

200<br />

0<br />

0.4<br />

0 2 4 6 8 10 12<br />

Reacti<strong>on</strong> Time (min)<br />

molecular weight<br />

iodine binding<br />

Figure 5. Change in the weight average molecular weight (Mw) and iodine binding of<br />

beta-limit dextrin when incubated with purified malt alpha-amylase under c<strong>on</strong>diti<strong>on</strong>s of<br />

the ASBC manual method for alpha-amylase.<br />

The sec<strong>on</strong>d porti<strong>on</strong> of the study focused <strong>on</strong> study of the reacti<strong>on</strong> of beta-limit dextrin<br />

with purified malt alpha- and beta-amylase. Malt alpha-amylase was purified from a<br />

crude Sigma (Sigma-Aldrich, St Louis) enzyme preparati<strong>on</strong> by heat shock and<br />

ultrafiltrati<strong>on</strong>. The freeze-dried enzyme preparati<strong>on</strong> was standardized to yield<br />

approximately 30, 60, and 90 DU in the manual method. Beta-amylase was from<br />

Megazyme (Ireland). In the first series of experiments the loss of iodine binding with<br />

alpha-amylase was m<strong>on</strong>itored both in the presence and absence of beta-amylase.<br />

2.2<br />

2.0<br />

1.8<br />

1.6<br />

1.4<br />

1.2<br />

1.0<br />

0.8<br />

0.6<br />

OD 650<br />

81

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