Enzymatic activities of Alternaria alternata allergenic extracts and its major allergen (Alt a 1)

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Abstract
Summary: Several allergens from Alternaria alternata have been isolated allowing some of them to be identified and characterised. Despite the fact that the major allergen of A. alternata (Alt a 1) has been extensively produced by recombinant technology, its biological activity still remains unknown. In the present study, extracts from culture filtrates were used to evaluate the intra‐specific variability of the enzymes and also as a source for isolating and purifying native Alt a 1. This was purified by affinity chromatography using antibody anti‐recombinant Alt a 1 (produced in Escherichia coli). Enzyme activities were analysed by the API‐ZYM System screening method. Results demonstrated the high variability of enzyme activities among the different strains. Only activities corresponding to phosphatases, esterases and β‐glucosidase were expressed by 100% of the strains. Both native and recombinant Alt a 1 showed phosphatase and esterase activities, suggesting that the glucidic moiety of this allergen does not significantly affect its enzyme activity.