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1.3.2 β-amylolysis (%)<br />

114<br />

β-amylase attacks the next to last glycosidic linkage from the<br />

non- reducing ends on branched chains and specifically releases maltose. However,<br />

this enzymatic action is blocked by α-D-(1,6) branched linkages (Zeikus, 1989). As<br />

shown in Figure 26, the debranched sample by 14 and 16 unit/g starch of pullulanase<br />

hydrolysis<br />

for 16 hr showed higher β-amylolysis (96.27 and 98.82 %) than did the 8<br />

to 12 unit/g starch concentration (66.60 to 83.48 %). These results indicated that the<br />

14 and 16 unit/g starch of pullulanase hydrolysis the rice starch was nearly completely<br />

debranched with 16 unit/g starch.<br />

Typically, the starch was completely debranched when it has<br />

been attacks by β-amylase at least about 95 %, more particularly at least about 98%,<br />

most particularly at least about 99 % debranched by weight (Nagamura el al. 2002).<br />

Beta-amylolusis (%)<br />

120<br />

100<br />

80<br />

60<br />

40<br />

20<br />

0<br />

0 8<br />

Figure 26 Effect of pullulanase enzyme concentration (0 to 16 unit/g starch) on<br />

β-amylolysis (%) of 16 hr debranching of 15% HARS preheated<br />

at 121°C for 30 min<br />

10 12 14 16<br />

Enzyme concentration (unit/g starch)

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