Enhanced secretion of heterologous cyclodextrin glycosyltransferase by a mutant ofBacillus licheniformisdefective in the D-alanylation of teichoic acids


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Abstract

Aims:To examine whether inactivation of the dlt operon and increased charge density of the wall enhances secretion of heterologous proteins in industrial strains of Bacillus licheniformis.Methods and Results:The dltA gene of B. licheniformis was cloned, sequenced and mutated by inserting a chloramphenicol acetyl transferase (cat) gene cassette. The mutation facilitated growth in the late exponential growth phase, increased endogenous autolysis and decreased resistance to a cationic peptide, polylysine. It was observed that dltA mutation increased the production of cyclodextrin glycosyltransferase (CGTase) by 1·5- to sevenfold depending on the growth phase, but decreased the production of penicillinase by twofold.Conclusions and Significance:The results suggest that the D-alanylation of teichoic acids is an element that can be used to improve the production of some secretory proteins in industrial applications based on this important industrial microorganism.

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