Galactomannan 이용에 관한 연구 I. Galactomannan에 대한 Pichia guilliermondii유래 $\alpha$-Galactosidase의 특이성

Specificity of Pichia guilliermondii $\alpha$-Galactosidase toward Galactomannans

  • 박귀근 (경원대학교 식품생물공학과)
  • 발행 : 1997.10.01

초록

$\alpha$-Galactosidase was partially purified from the culture filtrate of pichia guilliermondii by Mannobiose-Sepharose affinity column chromatography. The galactosidase exhibited maximum activity at pH 4.5 and 4$0^{\circ}C$, and was stable in the pH and temperature ranges of 4 to 5.5 and 30 to 6$0^{\circ}C$, respectively. The enzyme was inhibited by $Hg^{2+}$ and $Ag^{2+}$. The enzyme activity was ot affected considerably by treatment with other metal compounds. The enzyme hydrolyzed melibiose to galactose and glucose, raffinose to galactose and sucrose, and $Gal^{3}Man_{3}(6^{3}-$\alpha$-galactosyl-1,4-mannotriose)$ to galactose and mannotriose. On the contrary, it could not hydrolyze $Gal^{3}Man_{4}(6^{3}-galactosyl-1,4-$\alpha$-mannotetraose)$.

키워드

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