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Characterization Of Enzyme Allergens
The most thoroughly analyzed industrial enzyme is a -amylase derived from A.oryzae.Several proteins that bind to immunoglobulin E (IgE) have been detected in crude enzyme preparations, the dominating band having a molecular weight (MW) from 51 to 54 kDa (Quirce et al 1992, Baur et al 1994, Sandiford et al 1994, Houba et al 1997). The allergens were further studied, purified and identified (Baur et al 1994). A protein with a MW of 53 kDa was shown to represent the dominating allergen. The enzyme is a 478 amino-acid glycoprotein. The allergen was named Asp o 2. A xylanase from A.niger , used in baking additives, was shown to be allergenic, the allergen being ß -xylosidase of 105 kD (Sander et al 1998). Kim et al (1999) demonstrated that a cellulase preparation derived from T.viride and Fusarium moniliform had at least eight IgE binding components, the strongest band being at 56–63 kDa. The structure of an increasing number of environmental allergens has been determined (Aalberse 2000, Liebers et al 1996). Many of the allergens are functionally enzymes, for example, the allergens of flour, house dust mite and molds (Liebers et al 1996, Tiikkainen et al 1996, Houba et al 1998a, Sander et al 2001, Robinson et al 1997, Lake et al 1991, Robinson et al 1990). The proteolytic function of many of these allergens has been proposed to be an important factor in the epithelial permeability and origin of allergy (Robinson et al 1997, Kauffman et al 2000). Sandiford et al (1994) showed cereal amylases to be important allergens in patients with allergy to flour, but only minimal cross-reactivity was found between cereal amylases and fungal a-amylase.
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