Identification and application of new genes involved in glycosylation in koji mold

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Most of the enzymes from Aspergillus, including koji mold, are glycosylated, which improves both the functioning and efficacy of these enzymes. Although galactofuranose and glucose residues have been observed to be attached to the O-glycans and N-glycans of proteins in Aspergillus, the glycosyltransferase genes involved in the biosynthesis of these sugar residues have not yet been identified and the function of these sugar moieties also is not yet known1).The ability of filamentous fungi to secrete large quantities of proteins means that they are well suited for use as expression hosts for extragenous genes in industrial applications. However, since the sugar moieties of glycoproteins from filamentous fungi are antigenic in humans, they cannot be used for medicinal applications, such as antibody preparation. Consequently, a method for altering the structure of these sugar moieties needs to be developed so that a protein expression system using filamentous fungi can be developed.We therefore sought to identify the genes involved in the biosynthesis of these sugar moieties in filamentous fungi, and to elucidate the function of these sugar moieties in fungal growth and protein secretion.