Preparation Mechanism of Glycoprotein by Periodate-oxidized Soluble Starch and Maltooligosaccharides

과요오드산 산화당에 의한 인공단백질의 조제 메카니즘

  • Ann, Yong-Geun (Department of Food and Nutrition, Chungcheong College)
  • Published : 1999.04.30

Abstract

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.

과요오드산으로 산화시킨 당을 유리아미노산과 반응시켜서 ${\alpha}-NH_2$기와 펩티딜리신의 ${\varepsilon}-NH_2$기와 반응하여 결합한 것을 확인하였다. 그래서, 제조한 과요드산-산화당은 단백질 분자 표면의 리신의 ${\varepsilon}-NH_2$기와 Schiff 염기 반응으로 공유결합하여 당단백질을 만드는 것으로 볼 수 있다. 과요드산 산화당으로 변형한 고구마 ${\beta}$-아밀라아제는 C, H는 증가, N은 감소하였다. N말단의 ${\alpha}-NH_2$기는 70% (pentamer), 73% (monomer), ${\varepsilon}-NH_2$기는 33% (pentamer), 26% (monomer)가 산화당과 반응하였다. 페놀-황산법에 의한 총당 정량과 DNP 법으로 분석한 결과, $IO_4$-산화말토헥사오스는 고구마 ${\beta}$-아밀라아제 1몰당 6몰이 결합된 것으로 나타났고, 고구마 ${\beta}$-아밀라아제에 결합된 산화가용성 전분은 효소단백질 대비 13.2% (monomer), 13.5% (pentamer), 산화말토헥사오스는 9.7% (pentamer), 9.3% (monomer)로 나타났다.

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