Gel Promoting Ability of Various Gums and Purification of Trichoderma reesei α-Galactosidase by the Affinity chromatography

Affinity chromatography에 의한 Trichoderma reesei 유래 α-galactosidase의 정제 및 gum류의 증점효과

Park, Gwi-Geun
박귀근

  • Published : 20060000

Abstract

a-Galactosidase was purified from the culture filtrate of Trichoderma reesei by N-E-aminocaproyl-a-Dgalacto-pyranosylamin-sepharose affinity column chromatography. The galactosidase exhibited maximum acticity at 5.0 and 60°C, and was stable in the pH and temperature ranges of 3.0 to 6.0 and 20 to 60°C, respectively. The galactose/mannose ratio of guar gum(l: 1.6), guar gum treated with purified a-galactosidase and locust bean gum(I:3.3) were investigated. The galactose /mannose ratio of guar gum was changed 1:3.2 by the treatment of purified enzyme for 24 hI. Gel-promoting property of enzyme-treated guar gum was increased when the galactose/mannose ratio was about 1:3.2. An the ratio was appeared when the guar gum was hydrolyzed by the purified enzyme for 24 hr. It is clear that enzymatic depletion of galactose from guar gum by purified a-galactosidase would lead to a significant increase in gelation ability. And also mixture of xanthan gum and guar gum, and xanthan gum, guar gum and enzymetreated copra meal were investigated.

Keywords

References

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