Carrageenan is the main polysaccharide of red macroalgae and is composed of
d
-AHG and
d
-Gal. The carrageenan PUL (CarPUL)-encoded enzymes exist in many marine bacteria for decomposing carrageenan to provide self-growth. Here, the related enzymes in
Flavobacterium algicola
for metabolizing carrageenan were characterized for describing the catabolic pathways, notably, although the specific polysaccharide hydrolases existed that were like previous studies.
λ-Carrageenase with high activity is an effective
and environmentally
friendly tool enzyme for the preparation of λ-carrageenan oligosaccharides
with various biological activities. Herein, a novel GH150 (glycoside
hydrolases family 150) λ-carrageenase OUC-CglA from Maribacter vaceletii was heterologously expressed, purified,
and characterized. The recombinant OUC-CglA performs strict selectivity
toward λ-carrageenan with a specific activity of 418.7 U/mg
under its optimal reaction conditions of 20 °C and pH 7.0. Additionally,
OUC-CglA is a typical cold-adapted λ-carrageenase because it
unfolds 90% and 63% of its maximum activity at 15 and 10 °C,
respectively. The hydrolysis process suggests that OUC-CglA is an
endotype λ-carrageenase with the final products consisting of
λ-neocarrabiose, λ-neocarratetraose, λ-neocarrahexaose,
and other long-chain λ-neocarrageenan oligosaccharides. As a
result, high activity, cold-adaptation, and principal products of
OUC-CglA make it a potential biocatalyst for the effective preparation
of λ-carrageenan oligosaccharides.
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