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Alliinase appears to retain activity during garlic processing

Alliinase is an enzyme found in garlic that causes the conversion of alliin to allicin, the compound believed to be responsible for some of garlic's medicinal benefits. Although researchers have previously studied alliinase activity in fresh garlic, this is the first study to investigate its activity in dried, processed garlic. Researchers used gel filtration and affinity chromatography to isolate alliinase from commercially available garlic powder. The isolated enzyme exhibited slightly higher pH and temperature optima, compared to literature values for alliinase purified from fresh Allium sativum. When subjected to gel electrophoresis, the structure of the enzyme isolated from garlic powder appeared to be slightly modified, compared to enzyme from the intact plant. Despite this apparent difference, the alliinase in garlic powder retained its ability to convert both naturally occurring l-(+)-alliin and synthetic l-(+)-alliin to allicin.

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Krest I, Keusgen M. Quality of herbal remedies from Allium sativum: differences between alliinase from garlic powder and fresh garlic. Planta Med 1999; 65: 139-143.Alliinase appears to retain activity during garlic processing

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