Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1188311 | Food Chemistry | 2008 | 5 Pages |
Allinase, which catalyzes the conversion of alliin to allicin, the principal component of potential medicinal value in garlic, is a thermo-labile enzyme. The potential for allicin formation is determined by the quantity of allinase that remains active after the process of preserving garlic by drying. The kinetics of enzymatic activity loss during drying by temperature cycling or by constant temperature were evaluated and compared. Allicin-forming potential was 91% preserved by temperature cycling from 40 to 60 °C. It was found that sugars present in the garlic and the high molecular mass of the enzyme were responsible for protection against degradation at high drying temperatures. Preservation of the enzymatic activity under cyclical conditions occurred mainly with exposure to low temperatures for drying periods longer than those of constant drying conditions.