• The Korean Journal of Food And Nutrition
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• v.12 no.3
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• pp.265-270
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• 1999

The stabilization of Aspergillus sp. $\alpha$-amylase was attained by modification with periodate-oxidized sol-uble starch. The pH stability of modified enzyme was increased at pH 3~4 and 9~11 in the presence of $\alpha$-cyclodextrin($\alpha$-CD) compared with that of native enzyme. Thermal stability of the modified enzyme was increased. After treatment at 6$0^{\circ}C$ for 30min the activity remained 20% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD and tested in the presence of $\alpha$-CD 10% for the enzyme modified at pH 9.7 in the presence of $\alpha$-CD 0% for the native enzyme. The native enzyme and modified enzyme showed one peak in HPLC. The substrate specificity of the modified enzyme was not changed in HPLC analysis of reaction product.

• 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.