PURIFICATION AND SOME PROPERTIES OF A NOVEL ENDO-BETA-(1-]6)-D-GALACTANASE FROM ASPERGILLUS-NIGER

被引:25
作者
BRILLOUET, JM
WILLIAMS, P
MOUTOUNET, M
机构
[1] Institut National de la Recherche Agronomique, Institut des Produits de la Vigne, Laboratoire des Polymeres et des Techniques Physico-Chimiques, Montpellier, F-34060
来源
AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 06期
关键词
D O I
10.1080/00021369.1991.10870802
中图分类号
S3 [农学(农艺学)];
学科分类号
0901 ;
摘要
An endo-beta-(1 --> 6)-D-galactanase has been purified 26-fold (14% activity yield) from a crude enzyme preparation from Aspergillus niger. The enzyme was homogeneous on PAGE and SDS-PAGE, with an apparent molecular mass of 60 kDa. It has maximum activity at pH 3.5 on an enzymatically desarabinosylated grape 3,6-galactan-protein (Gp), being unreactive towards the native grape AGp. The enzyme liberated beta-(1 --> 6)-D-galactobiose and galactose in a final 1:0.26 molar ratio, beta-(1 --> 3)-D-galactosidic bonds being resistant to the action of enzyme.
引用
收藏
页码:1565 / 1571
页数:7
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