New enzymatic synthesis of 6(3)-modified maltooligosaccharides and their inhibitory activities for human alpha-amylases.

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作者信息

Uchida R, Nasu A, Tokutake S, Kasai K, Tobe K, Yamaji N

机构信息

Research and Development Division, Kikkoman Corporation, Chiba, Japan.

出版信息

Carbohydr Res. 1998 Feb;307(1-2):69-76. doi: 10.1016/s0008-6215(98)00029-9.

DOI:10.1016/s0008-6215(98)00029-9

PMID:9658564

Abstract

Ten new 6(3)-modified maltopentaoses and tetraoses were synthesized by enzymatic reactions utilizing cyclodextrin glycosyltransferase (EC 2.4.1.19) and subsequent human salivary alpha-amylase (HSA) (EC 3.2.1.1). Among these compounds, alpha-D-glucopyranosyl-(1-->4)- alpha-D-glucopyranosyl-(1-->4)-(6-deoxy-alpha-D-glucopyranosyl)-(1-->4)- alpha-D-glucopyranosyl-(1-->4)-D-glucopyranose (11) and alpha-D-glucopyranosyl-(1-->4)-(6-deoxy-alpha-D-glucopyranosyl)-(1-->4)- alpha-D-glucopyranosyl-(1-->4)-D-glucopyranose (12) showed strong inhibitory activities for human pancreatic alpha-amylase (HPA) and HSA. The IC50 of 6(3)-deoxymaltopentaose 11 (8.0 x 10(-5) M for HPA, 1.0 x 10(-4) M for HSA) and 6(3)-deoxymaltotetraose 12 (2.0 x 10(-3) M for HPA, 2.0 x 10(-3) M for HSA) were lower than that of 6(3)-deoxymaltotriose [(6-deoxy-alpha-D-glucopyranosyl)-(1-->4)-alpha-D- glucopyranosyl-(1-->4)-D-glucopyranose 13; 2.0 x 10(-3) M for HPA, 4.2 x 10(-2) M for HSA].

摘要