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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
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Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
Endohydrolysis of (1->4)-beta-linkages in the backbone of lambda-carrageenan, resulting in the tetrasaccharide alpha-D-Gal-p2,6S2-(1->3)-beta-D-Gal-p2S-(1->4)-alpha-D-Gal-p2,6S2-(1->3)-D-Gal-p2-S
proceeds according to an endolytic mode of action and a mechanism of inversion of the anomeric configuration
main reaction products, after prolonged incubation (22-50 h) increasing ratio of neo-lambda-carratetraose suggesting also the rise of a dimeric product arising from the cleavage of the hexamer
main reaction products, after prolonged incubation (22-50 h) increasing ratio of neo-lambda-carratetraose suggesting also the rise of a dimeric product arising from the cleavage of the hexamer
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, recombinant chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain from Escherichia coli strain BL21(DE3) by cellulose affinity chromatography using carbohydrate binding module in scaffoldin miniCbpA as a tag
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed as His-tag fusion protein in Escherichia coli, formation of inclusion bodies that are solved in 8 M urea; expression in Escherichia coli as insoluble inclusion bodies. These inclusion bodies are purified and solubilized in 8 M urea
subcloning in Escherichia coli strain DH5alpha, recombinant expression of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain in Escherichia coli strain BL21(DE3)
generation of a chimeric protein cCgkA and cCglA containing the catalytic domain of kappa-carrageenase CgkA and delta-carrageenase CglA fused with a dockerin domain, miniCbpA, cCgkA and cCglA assemble into a complex, the dockerin-fused enzymes on the scaffoldin have synergistic activity in the degradationof carrageenan showing enhancement of activity by carrageenolytic complex 3.1fold higher compared with the corresponding enzymes alone
the assemblies of advancement of active enzyme complexes, i.e. of kappa-carrageenase CgkA and delta-carrageenase CglA, will facilitate the commercial production of useful products from red algae biomass whichrepresents inexpensive and sustainable feed-stocks
Guibet, M.; Colin, S.; Barbeyron, T.; Genicot, S.; Kloareg, B.; Michel, G.; Helbert, W.
Degradation of lambda-carrageenan by Pseudoalteromonas carrageenovora lambda-carrageenase: a new family of glycoside hydrolases unrelated to kappa- and iota-carrageenases
Guibet, M.; Kervarec, N.; Genicot, S.; Chevolot, Y.; Helbert, W.
Complete assignment of 1H and 13C NMR spectra of Gigartina skottsbergii lambda-carrageenan using carrabiose oligosaccharides prepared by enzymatic hydrolysis