Aspergillus niger ATCC 16513과 대두(Glycine max. L)의 정제 $alpha$-galactosidase를 사용 하여 몇가지 이들의 kinetic성질을 조사 하였다. Asp. niger $alpha$-galactosidase의 raffinose와 stachyose에 대한 Km값은 각각 37.0mM과 55.5mM, 대두 $alpha$-galactosidase는 50.0mM과 55.5mM로서 PNPG보다 이들에 대한 친화성이 적었다. 또한 galactose는 ASP. niger와 대두 $alpha$-galactosidase 모두의 활성을 저해 하였으나 2-mereaptoethanol과 L-cystene은 대두 $alpha$-galatosidase의 활성만을 약간 저해 하였다. Asp. niger와 대두 $alpha$-galactosidase의 활성에 관여하는 아미노산은 diethyl pyrocarbonate에 의한 화학수식에 의하여 histidine임이 확인 되었고 Asp. niger $alpha$-galactosidase의 1mole당 아미노산 잔기수는 모두 902개, 대두$alpha$-galactosidase는 286개 이었다.
This experiment was carried out to elucidate some kinetic properties of the $alpha$-galactosidase which produced and purified from Aspergillus niger ATCC 16513 and soybean(Glycine max. L). The Km value of Asp. niger and soybean $alpha$-galactosidase were 37.0mM and 50.0mM for raffinose and55.5mM and 55.5mM for stachyose, respectively. The activity of Asp. niger and soybean $alpha$-galactosidase were inhibited by galactose. Among the amino acids in active sites of both Asp. niger and soybean $alpha$-galactosidase, histidine was identified by chemical modification of diethyl pyrocarbonate. Number of amino acids residues per mole of Asp. niger and soybean $alpha$-galactosidase were 902 and 286, respectively
