Xanthan-modifying enzymes are powerful tools in studying structure-function
relationships of this polysaccharide, One of these modifying enzymes is xa
nthan lyase, which removes the terminal side chain residue of xanthan. In t
his paper, the cloning and sequencing of the first xanthan lyase-encoding g
ene is described, i.e., the xalA gene, encoding pyruvated mannose-specific
xanthan lyase of Paenibacillus alginolyticus XL-1. The xalA gene encoded a
100,823-Da protein, including a 36-amino-acid signal sequence, The 96,887-D
a mature enzyme could be expressed functionally in Escherichia coli, Like t
he native enzyme, the recombinant enzyme showed no activity on depyruvated
xanthan, Compared to production by P. alginolyticus, a 30-fold increase in
volumetric productivity of soluble xanthan lyase was achieved by heterologo
us production in E. coli. The recombinant xanthan lyase was used to produce
modified xanthan, which showed a dramatic loss of the capacity to form gel
s with locust bean gum.