Physical state of κ-carrageenan modulates the mode of action of κ-carrageenase from <i>Pseudoalteromonas carrageenovora</i>

Lemoine, Maud; Collén, Pi Nyvall; Helbert, William

doi:10.1042/bj20080619

Cited by 31 publications

(20 citation statements)

References 50 publications

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“…The enzyme tended to preferentially release small ι-carrageenan fragments, suggesting a processive behavior consistent with other reported carrageenases [11], [13]. For a detailed analysis of the hydrolytic characteristics of CgiA_Ce, the main products of the CgiA_Ce were isolated by SEC on a Bio-Gel P6 column (Figure S1).…”

Section: Resultssupporting

confidence: 80%

Purification, Cloning, Characterization and Essential Amino Acid Residues Analysis of a New ι-Carrageenase from Cellulophaga sp. QY3

Duan

Chai

et al. 2013

PLoS ONE

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ι-Carrageenases belong to family 82 of glycoside hydrolases that degrade sulfated galactans in the red algae known as ι-carrageenans. The catalytic mechanism and some substrate-binding residues of family GH82 have been studied but the substrate recognition and binding mechanism of this family have not been fully elucidated. We report here the purification, cloning and characterization of a new ι-carrageenase CgiA_Ce from the marine bacterium Cellulophaga sp. QY3. CgiA_Ce was the most thermostable carrageenase described so far. It was most active at 50°C and pH 7.0 and retained more than 70% of the original activity after incubation at 50°C for 1 h at pH 7.0 or at pH 5.0–10.6 for 24 h. CgiA_Ce was an endo-type ι-carrageenase; it cleaved ι-carrageenan yielding neo-ι-carrabiose and neo-ι-carratetraose as the main end products, and neo-ι-carrahexaose was the minimum substrate. Sequence analysis and structure modeling showed that CgiA_Ce is indeed a new member of family GH82. Moreover, sequence analysis of ι-carrageenases revealed that the amino acid residues at subsites −1 and +1 were more conserved than those at other subsites. Site-directed mutagenesis followed by kinetic analysis identified three strictly conserved residues at subsites −1 and +1 of ι-carrageenases, G228, Y229 and R254 in CgiA_Ce, which played important roles for substrate binding. Furthermore, our results suggested that Y229 and R254 in CgiA_Ce interacted specifically with the sulfate groups of the sugar moieties located at subsites −1 and +1, shedding light on the mechanism of ι-carrageenan recognition in the family GH82.

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Section: Resultssupporting

confidence: 80%

Purification, Cloning, Characterization and Essential Amino Acid Residues Analysis of a New ι-Carrageenase from Cellulophaga sp. QY3

Duan

Chai

et al. 2013

PLoS ONE

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“…Enzymatic degradation of sulfated polysaccharides can be achieved by selecting enzymes such as hydrolases, fucoidanases (EC 3.2.1.44), α-L-fucosidases (EC 3.2.1.51) and galactosidases [96,103] to target glycosidic bonds while preserving the sulfate groups [100]. Fucoidanases and galactosidases have been identified in marine invertebrates and microorganisms [83,104,105,106,107,108]. Some bioactivities of lower molecular weight oligosaccharides prepared from algal sulfated polysaccharides are highlighted in Table 2.…”

Section: Approaches In Structural Analysis Of Algal Sulfated Polysmentioning

confidence: 99%

Chemical Structures and Bioactivities of Sulfated Polysaccharides from Marine Algae

et al. 2011

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Sulfated polysaccharides and their lower molecular weight oligosaccharide derivatives from marine macroalgae have been shown to possess a variety of biological activities. The present paper will review the recent progress in research on the structural chemistry and the bioactivities of these marine algal biomaterials. In particular, it will provide an update on the structural chemistry of the major sulfated polysaccharides synthesized by seaweeds including the galactans (e.g., agarans and carrageenans), ulvans, and fucans. It will then review the recent findings on the anticoagulant/antithrombotic, antiviral, immuno-inflammatory, antilipidemic and antioxidant activities of sulfated polysaccharides and their potential for therapeutic application.

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“…The kappa-carrageenase of P. carrageenovora adopts a β jelly-roll fold and displays a tunnel active site ( Figure 1A). These features suggest that this enzyme has an endo-processive mode of action (Michel et al 2001a), and this prediction has been biochemically confirmed (Lemoine et al 2009). …”

Section: Carrageenasesmentioning

confidence: 97%

Microorganisms living on macroalgae: diversity, interactions, and biotechnological applications

Martin

Portetelle

Michel

et al. 2014

Appl Microbiol Biotechnol

146

107

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Marine microorganisms play key roles in every marine ecological process, hence the growing interest in studying their populations and functions. Microbial communities on algae remain underexplored, however, despite their huge biodiversity and the fact that they differ markedly from those living freely in seawater. The study of this microbiota and of its relationships with algal hosts should provide crucial information for ecological investigations on algae and aquatic ecosystems. Furthermore, because these microorganisms interact with algae in multiple, complex ways, they constitute an interesting source of novel bioactive compounds with biotechnological potential, such as dehalogenases, antimicrobials and alga-specific polysaccharidases (e.g. agarases, carrageenases, alginate lyases). Here, to demonstrate the huge potential of alga-associated organisms and their metabolites in developing future biotechnological applications, we first describe the immense diversity and density of these microbial biofilms. We further describe their complex interactions with algae, leading to the production of specific bioactive compounds and hydrolytic enzymes of biotechnological interest.We end with a glance at their potential use in medical and industrial applications.

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Physical state of κ-carrageenan modulates the mode of action of κ-carrageenase from Pseudoalteromonas carrageenovora

Cited by 31 publications

References 50 publications

Purification, Cloning, Characterization and Essential Amino Acid Residues Analysis of a New ι-Carrageenase from Cellulophaga sp. QY3

Purification, Cloning, Characterization and Essential Amino Acid Residues Analysis of a New ι-Carrageenase from Cellulophaga sp. QY3

Chemical Structures and Bioactivities of Sulfated Polysaccharides from Marine Algae

Microorganisms living on macroalgae: diversity, interactions, and biotechnological applications

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