| abstract |
Disulfide proteins showed mitigated allergenicity and increased digestibility by pepsin following reduction by thioredoxin. The sulfhydryl groups newly formed on reduction by thioredoxin (at 4°C) or dithiothreitol (at 55°C) were blocked with a physiological disulfide, such as cystamine or oxidized glutathione to obtain stable forms of the disarmed allergen. Allergenicity of the two derivatives was compared with that of the oxidized, reduced and reoxidized forms of BLG by skin testing dogs from a colony sensitized to cow's milk. The reoxidized form resembled the derivatives in having lower allergenicity. Stable forms of such disarmed, hypoallergenic and hyperdigestible disulfide protein allergens or just hypoallergenic or just hyperdigestible protein allergens are useful foods as well as clinical preparations. |