Alginate Lyase in the Brown Alga Laminaria digitata (Huds.) Lamour.

Madgwick, J. C.; Haug, Arne; Lársen, Bjørn; Hedman, Kaj; Leander, Kurt; Swahn, Carl‐Gunnar

doi:10.3891/acta.chem.scand.27-0711

Cited by 42 publications

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“…The temperature of the sample cell (path length, I or 10 mm) was maintained at 2.0 or 2SoC and the sample compartment was flushed with nitrogen gas. The calculation was made in the way described by Adler et al 14 ) Ellipticity was expressed as mean residue ellipticity, (8), in deg cm 2 /decimol using a mean residue weight of llS.7 for SPI and 117.4 for SP2. Optical rotation, when Ao was taken to be 2I2nm, was expressed as reduced mean residue rotation, (m'), in deg cm 2 /decimol.…”

Section: T Muramatsu H Hashimoto and T Takahashimentioning

confidence: 99%

Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes fromTurbo cornutus

Muramatsu

Hashimoto

Takahashi

1984

Agricultural and Biological Chemistry

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Section: T Muramatsu H Hashimoto and T Takahashimentioning

confidence: 99%

Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes fromTurbo cornutus

Muramatsu

Hashimoto

Takahashi

1984

Agricultural and Biological Chemistry

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“…Because of its high viscosity and gelling properties with calcium ions, alginate is used widely in the food, pharmaceutical and medical industries. Alginate-depolymerizing enzymes have been isolated from fungi 198l), marine molluscs (Nakada & Sweeny, 1967;Nishizawa et al, 1968) and seaweeds (Madgwick et al, 1973;Shiraiwa et al, 1975). Most alginate lyase (ALY) * Author for correspondence.…”

Section: Introductionmentioning

confidence: 99%

Cloning, sequence analysis and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudomonas sp. OS-ALG-9

Maki

Mori²,

Fujiyama³

et al. 1993

Journal of General Microbiology

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“…[8][9][10][11] Alginate lyase is an alginate-degrading enzyme that splits alginate via a β-elimination reaction to produce oligosaccharides possessing an unsaturated sugar, 4-deoxy-L-erythro-hex-4-enopyranosyluronate, at the new non-reducing terminus. [2][3][4] Alginate lyases are distributed over brown algae, 12,13 herbivorous marine mollusks, [14][15][16][17][18][19][20][21][22] marine and soil bacteria 4,[23][24][25][26][27][28] and Chlorella virus. 29 According to the substrate preferences, alginate lyases are basically classified into poly(M) lyases (EC 4.2.2.3) and poly(G) lyases (EC 4.2.2.11), which are specific for poly(M)-block and poly(G)-block, respectively.…”

Section: Introductionmentioning

confidence: 99%

cDNA cloning and bacterial expression of a PL-14 alginate lyase from a herbivorous marine snail Littorina brevicula

Rahman

Wang

Inoue

et al. 2012

Carbohydrate Research

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Herbivorous marine snails like Littorina sp. are known to possess alginate lyases in their digestive tracts.The Littorina enzymes have been identified as endolytic polymannuronate (poly(M)) lyases (EC 4.2.2.3); however, it is still unclear which polysaccharide-lyase family (PL) the Littorina enzymes belong to, since no complete primary structure of Littorina enzymes has been determined. Thus, in the present study, we analyzed the primary structure of LbAly28, a 28 kDa alginate lyase isozyme of Littorina brevicula, by the cDNA method. LbAly28 cDNAs were amplified by PCR followed by 5'-and 3'-RACE PCRs from the L. brevicula hepatopancreas cDNA. A cDNA covering entire coding region of LbAly28 consisted of 1129 bp and encoded an amino-acid sequence of 291 residues. The deduced amino-acid sequence comprised an initiation methionine, a putative signal peptide of 14 residues, a propeptide-like region of 16 residues, and a mature LbAly28 domain of 260 residues. The mature LbAly28 domain showed 43-53% amino-acid identities with other molluscan PL-14 enzymes. The catalytically important residues in PL-14 enzymes, which were identified in the Chlorella virus glucuronate-specific lyase vAL-1 and Aplysia poly(M) lyase AkAly30, were also conserved in LbAly28. Site-directed mutagenesis regarding these residues, i.e., replacements of Lys94, Lys97, Thr121, Arg 123, Tyr135 and Tyr137 to Ala, decreased the activity of recombinant LbAly28 to various degrees. From these results we concluded that LbAly28 is a member of PL-14 alginate lyases. Besides the effects of above mutations, we noticed that the replacement of T121 by Ala changed the substrate preference of LbAly28. Namely, the activities toward sodium alginate and poly(MG)-block substrate increased and became comparable with the activity toward poly(M)-block substrate. This suggests that the region including T121 of LbAly28 closely relates to the recognition of poly(MG) region of alginate.3

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Alginate Lyase in the Brown Alga Laminaria digitata (Huds.) Lamour.

Cited by 42 publications

References 0 publications

Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes fromTurbo cornutus

Physicochemical Characteristics and Conformational Features of Alginate Lyase Isozymes fromTurbo cornutus

Cloning, sequence analysis and expression in Escherichia coli of a gene encoding an alginate lyase from Pseudomonas sp. OS-ALG-9

cDNA cloning and bacterial expression of a PL-14 alginate lyase from a herbivorous marine snail Littorina brevicula

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