Purification, characterization and sequencing of the major β-1,3-glucanase from the midgut of Tenebrio molitor larvae

Genta, Fernando Ariel; Bragatto, Ivan; Terra, Walter R.; Ferreira, Clélia

doi:10.1016/j.ibmb.2009.10.003

Cited by 52 publications

(50 citation statements)

References 61 publications

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“…2, marked in green) and 2 arginine residues and 1 histidine residue (Fig. 2, marked in blue) that help to modify the pKa of the catalytic glutamate residues (Genta et al, 2009;Kovalchuk et al, 2009;Song et al, 2010;Zakharenko et al, 2011). The predicted tertiary structure, produced from homology modelling of the putative amino acid sequences, had a β-jelly roll motif, which is also typical of family 16 glycosyl hydrolases (Genta et al, 2009) (Fig.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 98%

“…Like the sequences from C. destructor and G. natalis, the putative amino acid sequences contained the characteristic catalytic and binding domains of a glycosyl hydrolase family 16 protein (Juncosa et al, 1994;Genta et al, 2009) (Fig. 5).…”

Section: Sequences From Other Crabsmentioning

confidence: 99%

“…2, marked in yellow) and the correct catalytic and binding residues to be a catalytically active β-1,3-glucanase (Juncosa et al, 1994;Henrissat and Davies, 1997;Genta et al, 2009;Kovalchuk et al, 2009;Song et al, 2010). Both sequences contained features that are characteristic of glycosyl hydrolase family 16 enzymes, in particular the amino acid sequence "Glu-Ile-Asp-Ile-Val-Glu" (Fig.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

“…Both sequences contained features that are characteristic of glycosyl hydrolase family 16 enzymes, in particular the amino acid sequence "Glu-Ile-Asp-Ile-Val-Glu" (Fig. 2, marked in red); the first glutamate residue acts as the nucleophile, the second glutamate acts as the general acid base catalyst, while the aspartate acts to modify the pKa of the catalytic residues (Juncosa et al, 1994;Genta et al, 2009). The sequences also contain tryptophan substrate binding residues (Fig.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

“…(a) Gecarcoidea natalis Tenebrio molitor and Cryptopygus antarcticus, the secondary and tertiary structures of the β-1,3-glucanase from both G. natalis and C. destructor were highly similar to that of an endo-β-1,3-glucanase from Nocardiopsis sp strain f96 (Protein data bank code c2hykA) (Genta et al, 2009;Song et al, 2010). Compared to the amino acid sequence from Nocardiopsis, the respective similarity for that of G. natalis and C. destructor was 42 and 40%.…”

Section: G Natalis and C Destructor Ghf16 Sequencementioning

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: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 98%

Section: Sequences From Other Crabsmentioning

confidence: 99%

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

Section: G Natalis and C Destructor Ghf16 Sequencementioning

confidence: 99%

See 3 more Smart Citations

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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Cloning, expression, and functional analysis of the β‐1,3‐glucanase gene in Ostrinia furnacalis

Liu

Wang

Yang

et al. 2021

Biotech and App Biochem

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The β-1,3-glucanase gene in Ostrinia furnacalis was first obtained by RT-PCR. The real-time fluorescence quantitative PCR showed that the expression level of β-1,3-glucanase in the midgut of O. furnacalis was higher than in other tissues. Moreover, the expression level in the larval stage was higher in egg, pupa, and adult stages. The optimal pH of recombinant O. furnacalis β-1,3-glucanase OfLam to the substrate laminarin was 4.5, and the optimum reaction temperature was 50 • C. The enzyme exhibited a K M of 1.59 ± 0.28 mg/mL and a k cat of 15.8 ± 0.66 s -1 . Ostrinia furnacalis β-1,3-glucanase has a similar catalytic efficiency to other insect-derived β-1,3-glucanases. The recombinant OfLam has a broad substrate spectrum and can hydrolyze fungal cell walls, suggesting a new source of enzymes for biological control strategies that target fungal cell walls.

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Plant, Bacterial, and Fungal Cell Wall-Degrading Enzymes

Terra,

Ferreira,

Silva

2023

Entomology in Focus

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Purification, characterization and sequencing of the major β-1,3-glucanase from the midgut of Tenebrio molitor larvae

Cited by 52 publications

References 61 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

Cloning, expression, and functional analysis of the β‐1,3‐glucanase gene in Ostrinia furnacalis

Plant, Bacterial, and Fungal Cell Wall-Degrading Enzymes

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