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.
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 |
