• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.247-252
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• 1996

$\beta$-Amylase was purified from sweet potato by acetone fractlonatlon, Sephadex A-50 ion exchange chromatography and Sepgadex G-200 gel chromatographyl The higher enzyme concentration was, the higher heat stability of enzyme became. After 1 hour 30 minute. At 6$0^{\circ}C$ in pH 5, enzyme under concentration of 30$\mu$l/ml lost its activity completely and over the concentration of 100$\mu$g/ml remained 25% of activity. The enzyme was stabilized at range of pH 4~10 and pH stability was increased by glycerol. Five moles of NaCl inhibited completely of the enzyme activity. SDS of 0.05% inhibited the enzyme completely after 12 hours at 37$^{\circ}C$ in pH5. One mole guanidine-HCl and 8M urea inhibited the entire enzyme after 13 hours at 37$^{\circ}C$ in pH 5.

• The Korean Journal of Food And Nutrition
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• v.9 no.3
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• pp.253-258
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• 1996

Stabilities of sweets potato f-amylase on various reagents were studied. The enzyme was stabilized by bovine serum albumin, Triton X-100 and 2-mercaptoethanol of 0.04%. Among them, bovine serum albumin was the most effective. And enzyme stability was increased by using the deairated solution. The enzyme activity was remained 0% in the absence of glycerol, 25% in the presence of 20% glycerol and 50% in the presence of 40% glycerol at 37$^{\circ}C$, for 15 hours in pH 11. SDS inhibited the enzyme, and 2-mercaptoethanol and dithiothreitol stabilized it.

• The Korean Journal of Food And Nutrition
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• v.11 no.5
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• pp.561-564
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• 1998

The stabilizatio of amaylolytic enzyme such as $\beta$-amylase of barley, $\beta$-amylase of wheat, $\beta$-amylase of sweet potato, $\alpha$-amylase of Bacillus licheniformis, $\alpha$-amylase of Aspergillus sp. and $\alpha$-glucosidase of Aspergillus awamori was attained by modification with periodate-oxidized soluble starch. The pH stability of modified enzyme was increased at pH 9 for $\beta$-amylase of sweet potato, pH 3~5 and 8~11 for $\beta$-amylase of barley, pH 2~3 and 7~12 for $\beta$-amylase of wheat and pH 6 for $\alpha$-glucosidase of Aspergillus awamori. Thermal stability increased 17.6% for $\alpha$-amylase of Aspergillus sp. at 6$0^{\circ}C$ for 10min, 30% for $\alpha$-amylase of Bacillus licheniformis at 10$0^{\circ}C$ for 5min and 4.5% for $\alpha$-amylase of sweet potato at 6$0^{\circ}C$ for 10min compared with those of native enzymes.

• The Korean Journal of Food And Nutrition
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• v.11 no.2
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• pp.159-164
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• 1998

pH stability of sweet potato $\beta$-amylase modified with IO4-oxidized soluble starch was increased at pH 3, 5~9 and 11. And optimum pH was 3 and 5 for modification. Thermal stability of the enzyme modified with IO4-oxidized soluble starch was increased at 6$0^{\circ}C$ for 15 min. pH stability of barley $\beta$-amylase modified with IO4-oxidized soluble starch was increased at 3~4 and 8~11, and more increased at pH 3 and 8~11 in the presence of $\alpha$-cyclodextrin.