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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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
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
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
kappa-, iota- and lambda-carrageenase display strict specificity for their substrates, namely kappa-, iota- and lambda-carrageenans, respectively. The enzymes discriminate the substrate probably by recognizing the sulfation pattern of the digalactose reapeting unit of the polysaccharide. lambda-Carrageenas present conserved arginine residues in the catalytic site which are believed to interact with carrageenans in which both sugar residues in the disaccharide units are negatively charged
the most important types of commercial carrageenans, namely kappa-, iota- and lambda-carrageenan, are esterified with one, two, and three sulfate groups per repeating disaccharide unit, being also called carrageenose 4'-sulfate, carrageenose 2,4'-disulfate, and carrageenose 2,6,2'-trisulfate, respectively. kappa-Carrageenans occur in the cell wall of some species of marine red algae, such as Chondrus sp., Gigartina sp., Eucheuma sp. and Iridaea sp. but is mostly extracted from tropical seaweed Euchema cottoni (also known as Kappaphycus alvarezii), while iota-carrageenans are mainly extracted from Eucheuma spinosum (also known as Eucheuma denticulatum). Because kappa- and iota-carrageenans are produced from my- and ny-carrageenans, respectively, during the extraction under alkaline at high temperatures or biosynthetically by a reaction catalyzed by the enzyme sulfohydrolase, these polysaccharides are often found in commercial samples. lambda-Carrageenans are extracted from red algae within the Gigartina and Chondrus genera, which produces this type of polysaccharide during the sporophytic stage. These algae are also a source of kappa- and iota-carrageenans when they are in the gametophytic stage, but because they produce mixed chain polysaccharide chains containing both kappa- and iota-units, extraction of kappa- and iota-carrageenans from the mentioned algae is preferred. Carrageenan classes based on the number and position of sulfate groups in the chain, overview. The sulfate and AD contents of commercial kappa-, iota-, and lambda-carrageenans have been determined by acid hydrolysis, infrared spectroscopy, and nuclear magnetic resonance (NMR) analyses and found to be, respectively, 25-30 and 28-35% for the kappa-type, 28-30 and 25-30% for iota-type and 32-39% and 0 for lambda-type, respectively
lambda-carrageenases belong to a to date unclassified GH family in the carbohydrateactive enzymes (CAZy) database. In spite of having specificities for structure-related substrates, kappa-, iota- and lambda-carrageenases do not share significant sequence homology, although all of them share some common binding site for ions important in stabilizing the enzyme
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
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)
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
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3.2.1.162 lambda-carrageenase
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