Extracellular soluble polysaccharide (ESP) from Aspergillus kawachii improves the stability of extracellular beta-gluocosidases (EX-1 and EX-2) and is involved in their localization.

Aspergillus kawachii produces two extracellular beta-glucosidases (EX-1 and EX-2) and one cell-wall-bound beta-glucosidase (CB-1), all of which are derived from the same bglA gene. Extracellular beta-glucosidases (EX-1 and EX-2) are stable in the crude solution form, but become unstable in the purified form under moderate conditions (pH 5.0 and 37 degrees C). Purified extracellular beta-glucosidases can bind to a mycelial cell wall fraction, even though these enzymes are released into the medium under solid culture conditions. A. kawachii produces an extracellular soluble the beta-glucosidases over the pH range of 3.0-7.0 and at temperatures below 50 degrees C. ESP directly interacted with the purified extracellular beta-glucosidases but did not affect the K(m) values of these enzymes. Moreover, ESP inhibited the adsorption of purified extracellular beta-glucosidases to the cell wall fraction and extracted them from it. These results that ESP plays important roles in the stability and localization of extracellular beta-glucosidases. ESP from A. kawachii directly binds to the enzymes and releases them to the medium from the cell wall layer and then stabilizes them.