Abstract
We evaluated the effects of cooking conditions and hot -holding to tenderize chicken, based on the action of ginger protease on collagen which occurs only in the telopeptide region under acidic conditions and not in the triple-helical region.
The acid-soluble and pepsin-solubilized collagen (ASC and PSC) contents in the chicken samples decreased with cooking, but the amount of insoluble collagen (ISC) increased. Hot-holding the cooked chicken samples decreased the total amount of collagen, as did ginger juice when added to the heated samples. This was probably because ginger protease acted on the thermally denatured regions of collagen with an irregular structure resulting from cooking and hot-holding. The addition of ginger juice significantly decreased the shear force of the cooked chicken samples in comparison with the other samples without added ginger juice.
