The Biochemistry of Laminarin and the Nature of Laminarinase

Bull, Alan T.; Chesters, C. G. C.

doi:10.1002/9780470122730.ch5

Cited by 28 publications

(17 citation statements)

References 133 publications

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“…Hydrolysis of β-1,3-glucans as a source of glucose β-1,3-glucanase is an enzyme that can hydrolyse β-1,3-glucans such as laminarin and callose. Laminarin is the major storage polysaccharide within brown algae and callose and is produced in plants in response to wounding (Bull and Chesters, 1966;Bacic et al, 1988). β-1,3-glucans are also present in other organisms such as diatoms, protozoans and fungi (Bull and Chesters, 1966;Piavaux, 1977;Bacic et al, 1988;Ruiz-Herrera, 1992;Terra and Ferreira, 1994;Pesentseva et al, 2008).…”

Section: Function Of the Ghf16 Proteinmentioning

confidence: 99%

“…Laminarin is the major storage polysaccharide within brown algae and callose and is produced in plants in response to wounding (Bull and Chesters, 1966;Bacic et al, 1988). β-1,3-glucans are also present in other organisms such as diatoms, protozoans and fungi (Bull and Chesters, 1966;Piavaux, 1977;Bacic et al, 1988;Ruiz-Herrera, 1992;Terra and Ferreira, 1994;Pesentseva et al, 2008). In species such as Petrolisthes elongatus and Metapenaeus bennetae that consume algae and possess high activities of β-1,3-glucanase, this enzyme would hydrolyse and thus digest β-1,3-glucans to produce mainly glucose (Johnston and Freeman, 2005;Allardyce and Linton, 2008;Figueiredo and Anderson, 2009).…”

Section: Function Of the Ghf16 Proteinmentioning

confidence: 99%

“…It catalyses the hydrolysis of β-1,3-glycosidic bonds within β-1,3-glucans such as laminarin and callose. Laminarin is the major storage polysaccharide in brown algae (Bull and Chesters, 1966), diatoms (Pesentseva et al, 2008) and protozoans (Piavaux, 1977) while callose is present in the wound tissue of plants (Bacic et al, 1988;Ruiz-Herrera, 1992;Terra and Ferreira, 1994).…”

Section: Introductionmentioning

confidence: 99%

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A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton

Cameron

Gray

et al. 2015

Gene

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To identify the gene responsible for the production of a β-1,3-glucanase (laminarinase) within crustacea, a glycosyl hydrolase family 16 (GHF16) gene was sequenced from the midgut glands of the gecarcinid land crab, Gecarcoidea natalis and the freshwater crayfish, Cherax destructor. An open reading frame of 1098 bp for G. natalis and 1095 bp for C. destructor was sequenced from cDNA. For G. natalis and C. destructor respectively, this encoded putative proteins of 365 and 364 amino acids with molecular masses of 41.4 and 41.5 kDa. mRNA for an identical GHF16 protein was also expressed in the haemolymph of C. destructor. These putative proteins contained binding and catalytic domains that are characteristic of a β-1,3-glucanase from glycosyl hydrolase family 16. The amino acid sequences of two short 8-9 amino acid residue peptides from a previously purified β-1,3-glucanase from G. natalis matched exactly that of the putative protein sequence. This plus the molecular masses of the putative proteins matching that of the purified proteins strongly suggests that the sequences obtained encode for a catalytically active β-1,3-glucanase. A glycosyl hydrolase family 16 cDNA was also partially sequenced from the midgut glands of other amphibious (Mictyris platycheles and Paragrapsus laevis) and terrestrial decapod species (Coenobita rugosus, Coenobita perlatus, Coenobita brevimanus and Birgus latro) to confirm that the gene is widely expressed within this group. There are three possible hypothesised functions and thus evolutionary routes for the β-1,3-glucanase: 1) a digestive enzyme which hydrolyses β-1,3-glucans, 2) an enzyme which cleaves β-1,3-glycosidic bonds within cell walls to release cell contents or 3) an immune protein which can hydrolyse the cell walls of potentially pathogenic micro-organisms.

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Section: Function Of the Ghf16 Proteinmentioning

confidence: 99%

Section: Function Of the Ghf16 Proteinmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Linton

Cameron

Gray

et al. 2015

Gene

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“…One unit of lipase activity was defined as the amount of enzyme that released μmol fatty acid per min in the assay conditions. β β β β β1-3 Glucanase activity β1-3 Glucanase was determined at pH 7.0/40ºC in 0.1M citrate-phosphate buffer (2). A unit of activity was defined as the amount of enzyme that released 1 μg of glucose in 20 min in the assay conditions.…”

Section: Lipase Activitymentioning

confidence: 99%

Technological application of an extracellular cell lytic enzyme in xanthan gum clarification

Shastry¹,

Prasad²

2005

Braz. J. Microbiol.

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An extracellular cell lytic enzyme from Pseudomonas sp. was active on heat killed cells of Xanthomonas campestris. The lytic activity caused enzymatic digestion of X.campestris xanthan gum. Digestion was effective for highly viscous native xanthan 2.0% (w/v) and 2.5% (w/v) commercial Sigma xanthan. Scanning electron microscopy and SDS-PAGE observations confirmed the cell lytic action on X.campestris cells.

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“…The content of laminarin in brown algae is up to 32%-35% of dry weight in Laminaria digitata, Laminaria hyperborea, and Saccharina latissima and these values change seasonally [4]. To date, laminarinases are found in some species of bacteria, fungi, yeasts, and marine invertebrates [5].…”

Section: Introductionmentioning

confidence: 99%

Continuous Saccharification of Laminarin by Immobilized Laminarinase ULam111 Followed by Ethanol Fermentation with a Marine-Derived Yeast

Mitsuya¹,

Yamamoto²,

Okai³

et al. 2017

AiM

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We isolated a novel laminarinase ULam111 from Flavobacterium sp. strain UMI-01. Purified ULam111 showed degradation activity against laminarin with the specific activity of 224 ± 18 U/mg at 30˚C and pH 6.0. Its optimum temperature was 50˚C, and degradation activities against laminarin were observed at 4˚C -80˚C. With a laminarin degradation system, we investigated the preparation and properties of immobilized ULam111 with the use of the 11 types of carriers. The high activity recoveries of immobilized ULam111 were as follows: 19.4% for IB-S60P carrier beads (the non-ionic type), 15.6% for IB-S60S carrier beads (the non-ionic type), 11.9% for IB-150P carrier beads (the covalent type), and 7.1% for IB-C435 carrier beads (the cationic type). With the repeated use of immobilized ULam111, the enzyme activities immobilized on IB-S60S and those on IB-S60P remained at 40% and 30% respectively after the sixth trial. We selected IB-S60S as suitable beads for enzyme immobilization, and we attempted to construct a reactor system with ULam111 immobilized on IB-S60S beads. In this system, 1.2 -1.9 g/L glucose was repeatedly produced from 30 mg/mL laminarin solutions after 20 hr when the reactor operation was repeated 10 times. We examined ethanol fermentation from the saccharified solutions with a marine-derived yeast (Saccharomyces cerevisiae C-19), and 0.51 -0.58 g/L bioethanol was produced from the saccharified solution that contained 1.71 -1.86 g/L of glucose.

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The Biochemistry of Laminarin and the Nature of Laminarinase

Cited by 28 publications

References 133 publications

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

A glycosyl hydrolase family 16 gene is responsible for the endogenous production of β-1,3-glucanases within decapod crustaceans

Technological application of an extracellular cell lytic enzyme in xanthan gum clarification

Continuous Saccharification of Laminarin by Immobilized Laminarinase ULam111 Followed by Ethanol Fermentation with a Marine-Derived Yeast

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