A beta-rutinosidase from Penicillium rugulosum IFO 7242 that is a peculiar flavonoid glycosidase.
A beta-rutinosidase, which was specific for releasing the disaccharide rutinose from the flavonoid glycoside rutin, was purified from Penicillium rugulosum IFO 7242. This enzyme had the molecular weight of 245,000, a very low optimum pH of 2.2, and the remarkable specificity that the glycosidase did not hydrolyze any other substrates like 4-nitrophenyl beta-glucoside and cellobiose, but only rutin and isoquercitrin.
Narikawa
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T
Graduate School of Science and Technology, Faculty of Horticulture, Chiba University, Matsudo-shi, Japan.
Shinoyama
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H
Fujii
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T
D006026:Glycoside Hydrolases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D008970:Molecular Weight; D010407:Penicillium / Q000201:enzymology*; D011794:Quercetin / Q000031:analogs & derivatives; D012431:Rutin; D013379:Substrate Specificity
C016527:isoquercitrin; D012431:Rutin; D011794:Quercetin; D006026:Glycoside Hydrolases; C416847:beta-rutinosidase