Abstract

An Escherichia coli recombinant system produced soluble and full-length ?-1,3-glucanase type II (BglII) cloned from the yeast-lytic actinomycete Oerskovia xanthineolytica. The expression system was designed to produce recombinant BglII with a six-histidine peptide fused to the carboxy end of the protein. The expression level was optimized to produce 30% of total protein of E. coli as the recombinant protein, releasing 75% to the extracellular space. The 43-kDa recombinant protein was purified by IMAC to homogeneity and its molecular and biochemical characteristics were studied, showing that there are no important functional differences with those properties described for the BglII purified from O. xanthineolytica. © 2001 Academic Press.