Academic Journals Database
Disseminating quality controlled scientific knowledge

Partial Purification and Characterization of α and β-Amylases Isolated from Sorghum bicolor cv. (Feterita) Malt

Author(s): Mawahib E.M. El Nour | S.O. Yagoub

Journal: Journal of Applied Sciences
ISSN 1812-5654

Volume: 10;
Issue: 13;
Start page: 1314;
Date: 2010;
VIEW PDF   PDF DOWNLOAD PDF   Download PDF Original page

Keywords: a and B-amylases | sorghum malt | storage stability | Diastatic power | enzymes temperature | pH

The research aimed to study the diastatic power (PD) of sorghum malt , to purify the α and β-amylase s and to characterize these enzymes. In this study the amylolytic activity initiated during the germination of sorghum was determined. Fourth day of germination of sorghum grains showed the highest of the amount of Diastatic Power (DP) (62.0 IOB), no significant variation (p≤0.05) between the extraction procedures followed either by distilled water or water with 2% peptone. DEAE-cellulose chromatography was used for the partial purification of α-and β-amylases. The results obtained from the last purification steps is 6.94 fold of α-amylase in fifth day of germination, whereas β-amylase is 35.42 fold in fourth day of germination. These amylases isolated from sorghum malt have interesting characteristics such as, storage stability of purified α and β-amylases at different temperature (-20 and 4°C) for 56 days. No significant loss (p≤0.05) in the enzymes activity during the storage period for 56 days in-20°C, whereas the loss of enzyme activity at 4°C during the period of 56 days were 19% for α and 34% for β-amylases. The maximum activity of α-amylase was obtained at temperature 70 and 50°C for β-amylase, it was clear that the α-amylase is more stable than β-amylase. The optimum pH for both α and β-amylases were 5.0 and 5.5, respectively. Therefore, these characterizations meet the prerequisites need for food industry.
Affiliate Program     

Tango Rapperswil
Tango Rapperswil