The xanthan-degrading bacterium Paenibacillus alginolyticus XL-1, isolated
from soil, degrades approximately 28% of the xanthan molecule and appears t
o leave the backbone intact. Several xanthan-degrading enzymes were excrete
d during growth on xanthan, including xanthan lyase. Xanthan lyase producti
on was induced by xanthan and inhibited by glucose and low-molecular-weight
enzymatic degradation products from xanthan. A xanthan lyase with a molecu
lar mass of 85 kDa and a pI of 7.9 was purified and characterized. The enzy
me is specific for pyruvated mannosyl side chain residues and optimally act
ive at pH 6.0 and 55 degrees C.