Chitin is an abundant natural polysaccharide
that is hard to degrade
because of its crystalline nature and because it is embedded in robust
co-polymeric materials containing other polysaccharides, proteins,
and minerals. Thus, it is of interest to study the enzymatic machineries
of specialized microbes found in chitin-rich environments. We describe
a genomic and proteomic analysis of
Andreprevotia ripae
, a chitinolytic Gram-negative bacterium isolated from an anthill.
The genome of
A. ripae
encodes four secreted
family GH19 chitinases of which two were detected and upregulated
during growth on chitin. In addition, the genome encodes as many as
25 secreted GH18 chitinases, of which 17 were detected and 12 were
upregulated during growth on chitin. Finally, the single lytic polysaccharide
monooxygenase (LPMO) was strongly upregulated during growth on chitin.
Whereas 66% of the 29 secreted chitinases contained two carbohydrate-binding
modules (CBMs), this fraction was 93% (13 out of 14) for the upregulated
chitinases, suggesting an important role for these CBMs. Next to an
unprecedented multiplicity of upregulated chitinases, this study reveals
several chitin-induced proteins that contain chitin-binding CBMs but
lack a known catalytic function. These proteins are interesting targets
for discovery of enzymes used by nature to convert chitin-rich biomass.
The MS proteomic data have been deposited in the PRIDE database with
accession number PXD025087.