Abstract

An Escherichia coli recombinant system produced a soluble ?-1,3-glucanase (BglII) cloned from Oerskovia xanthineolytica. The protein was obtained in a truncated form derived from the complete polypeptide. Cell fractionation studies show that 80% of the glucanase was retained in the periplasmic space after 20 h of induction. If cells were grown with glycine, 60% of the glucanase was released from the periplasm.