A number of Sphingomonas strains capable of synthesizing the bacterial
exopolysaccharide gellan and related polymers were shown to possess c
onstitutive gellanase activity. In each case, the degradation of deacy
lated gellan was due to extracellular, eliminase-type enzymes (lyases)
which cleave the sequence ...beta-D-glucosyl 1,4-beta-D-glucuronosyl.
.. in the tetrasaccharide repeat unit of the substrate polysaccharides
. Deacetylated rhamsan was an alternative substrate but there was litt
le or no action against most other polysaccharides with similar struct
ures. Slight differences were found between the specificities of the l
yases from different strains. Activities of gellan lyase preparations
were generally low. As well as the extracellular 'gellanase' activity,
all the bacteria possessed varying amounts of beta-D-glucosidase and
beta-D-glucuronidase activities apparently located in the periplasm. T
he products from deacylated gellan and the chemically deacylated form
of polysaccharide S194 (rhamsan gum), which is effectively a gentiobio
sylated form of gellan, closely resembled those recently obtained by t
he authors from other, gellan-degrading, non-gellan-producing bacteria
. The enzymes had negligible activity against the natural, acylated ge
llan and rhamsan polysaccharides from bacteria now designated as strai
ns of Sphingomonas.