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KMID : 1160619980030020152
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Preventive Nutrition and Food Science
1998 Volume.3 No. 2 p.152 ~ p.156
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Partial Purification and Characterization of a Soluble β-Fructoguracosidase from Onion (Allium cepa)
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Lee Yong-Eok
Yoo Jin-Young
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Abstract
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A fructan-degrading enzyme was partially purified from onion (Allium cepa) bulbs by a combination of ammonium sulfate precipitation, concanavalin-A affinity chromatography, and ion-exchange and gel-filtration chromatography. The enzyme hydrolyzed sucrose more effectively than inulin and was identified as a β-fructofuranosidase (invertase). The optimum pH and temperature were pH 5.5 and 35℃, respectively. The enzyme hydrolyzed sucrose with a K_m of 1.2 mM. The soluble β-fructofuranosidase is likely glycoprotein based on its ability to bind the lectin concanavalin-A. The enzyme was heatlabile, with most activity being lost at 50℃ in 1 hr of incubation. The onion β-fructofuranosidase was partially inhibited by ZnCl2, HgCl2 and CuSO4.
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KEYWORD
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onion, purification, β-fructofuranosidase
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