• Korean Journal of Food Science and Technology
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• v.31 no.2
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• pp.482-487
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• 1999

Periodate-oxidized soluble starch and maltohexaose reacted with ${\alpha}-NH_2$ group of free amino acids and ${\varepsilon}-NH_2$ group of peptidyl lysine. The result shows that periodate-oxidized soluble starch and maltooligosaccharides reacted with protein and formed Schiff base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of surface lysine of protein molecule. Carbon and hydrogen composition of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch increased and it's nitrogen composition decreased. Carbohydrate contents of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch were 13.2% (pentamer), 13.4% (monomer), and with oxidized maltohexaose were 9.7% (pentamer), 9.3% (monomer) by $phenol-H_2SO_4$ method. Alpha-amino group of N-terminal, and ${\varepsilon}-NH_2$ group of lysine, of sweet potato ${\beta}-amylase$ were reacted with oxidized soluble starch by dinitrophenylation were 70% (pentamer), 73% (monomer) and 33% (pentamer), 26% (monomer), respectively, in comparison with native enzyme.

• Korean Journal of Food Science and Technology
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• v.31 no.1
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• pp.62-67
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• 1999

Periodate-oxidized soluble starch and maltohexaose, maltotetraose, maltose, and glyceraldehyde reacted with sweet potato ${\beta}-amylase$, wheat ${\beta}-amylase$, aldolase, bovine serum albumin, catalase, carboxypeptidase, ferritin and pronase. Electrophoretical mobility of modified proteins was different from that of native proteins, and modified proteins were stained with periodic acid-Schiff while native proteins did not stain. This results means that oxidized sugars attached on proteins. This bond is based on the Schiffs base between CHO group of oxidized sugar and ${\varepsilon}-NH_2$ group of lysine of protein. There is no changed UV absorption spectrum of sweet potato ${\beta}-amylase$ modified with oxidized soluble starch, in comparison with native enzyme.