ʲ-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme

Arcand, Normand; Kluepfel, Dieter; Paradis, F. W.; Morosoli, Rolf; Shareck, François

doi:10.1042/bj2900857

Cited by 87 publications

(71 citation statements)

References 22 publications

(38 reference statements)

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“…b-1,4-Mannanases (E.C.3.2.1.78), catalyzing the hydrolysis of the b-1,4 glycosidic linkages in mannan, galactomannan, glucomannan and galactoglucomannan [4,5], have been purified and characterized from several different sources such as plants, fungi and bacteria [6][7][8][9][10][11]. For some of the b-mannanases, the cDNA sequences have been determined.…”

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confidence: 99%

Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β‐mannanase gene

Sellos

Janson

2002

European Journal of Biochemistry

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Using PCR, cloning and sequencing techniques, a 1.1-kb complementary DNA fragment encoding for a b-mannanase (mannan endo-1,4-b-mannosidase, EC 3.2.1.78) has been identified in the digestive gland of blue mussel, Mytilus edulis. The cDNA sequence shows significant sequence identity to several b-mannanases in glycoside hydrolase family 5. The b-mannanase gene has been isolated and sequenced from gill tissue of blue mussel and contains five introns. The b-mannanase has been expressed extracellularly in Pichia pastoris using the Saccharomyces cerevisiae a-factor signal sequence. The b-mannanase was produced in a 14-L fermenter with an expression level of 900 mgAEL. The expression level is strongly affected by the induction temperature. A two-step purification procedure, composed of a combination of immobilized metal ion affinity chromatography and ion exchange chromatography, is required to give a pure b-mannanase. However, due to post-translational modifications, structural varieties regarding molecular mass and isoelectric point were obtained. The specific activity of the purified recombinant M. edulis b-mannanase was close to that of the wild-type enzyme. Also pH and temperature optima were the same as for the native protein.In conclusion, P. pastoris is regarded as a suitable host strain for the production of blue mussel b-mannanase. This is the first time a mollusc b-mannanase has been characterized at the DNA level.

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confidence: 99%

Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β‐mannanase gene

Sellos

Janson

2002

European Journal of Biochemistry

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“…The three conserved active site residues (Asn-121, Glu-122, and Glu-223) and the strictly conserved residues Arg-43, His-80, His-188, Tyr-190, and Trp-248 that are characteristic of all family 5 enzymes (2, 4, 20, 28, 49) were also found in ManAd3. The mannanase domain of ManA exhibited 71% sequence identity with the mannanase catalytic domains of ManA and CelC of Caldicellulosiruptor saccharolyticus (19,33) and 56% sequence identity with the ␤-mannanase ManA of Streptomyces lividans (1).…”

Section: Resultsmentioning

confidence: 99%

A Gene Encoding a Novel Multidomain β-1,4-Mannanase from Caldibacillus cellulovorans and Action of the Recombinant Enzyme on Kraft Pulp

Sunna

Gibbs

Chin

et al. 2000

Appl Environ Microbiol

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Genomic walking PCR was used to obtained a 4,567-bp nucleotide sequence from Caldibacillus cellulovorans. Analysis of this sequence revealed that there were three open reading frames, designated ORF1, ORF2, and ORF3. Incomplete ORF1 encoded a putative C-terminal cellulose-binding domain (CBD) homologous to members of CBD family IIIb, while putative ORF3 encoded a protein of unknown function. The putative ManA protein encoded by complete manA ORF2 was an enzyme with a novel multidomain structure and was composed of four domains in the following order: a putative N-terminal domain (D1) of unknown function, an internal CBD (D2), a ␤-mannanase catalytic domain (D3), and a C-terminal CBD (D4). All four domains were linked via proline-threonine-rich peptides. Both of the CBDs exhibited sequence similarity to family IIIb CBDs, while the mannanase catalytic domain exhibited homology to the family 5 glycosyl hydrolases. The purified recombinant enzyme ManAd3 expressed from the cloned catalytic domain (D3) exhibited optimum activity at 85°C and pH 6.0 and was extremely thermostable at 70°C. This enzyme exhibited high specificity with the substituted galactomannan locust bean gum, while more substituted galacto-and glucomannans were poorly hydrolyzed. Preliminary studies to determine the effect of the recombinant ManAd3 and a recombinant thermostable ␤-xylanase on oxygen-delignified Pinus radiata kraft pulp revealed that there was an increase in the brightness of the bleached pulp.The use of hemicellulases in the manufacture of kraft pulp has been shown to promote pulp bleaching, and in most application studies the workers have focused on using xylanases (24,47,48). Using mannanases was not studied until recently, when it was shown that mannanases, acting in combination with xylanases, enhance enzyme-aided bleaching of pulps in modified kraft processes (10, 40).1,4-␤-Mannans, which are some of the major constituents of hemicellulose, are hydrolyzed to mannose by endo-acting ␤-mannanases and exo-acting ␤-mannosidases. However, due to the complexity of the polysaccharide and the presence of side chain sugars, additional enzymes, including ␣-galactosidase, ␤-glucosidase, and acetylmannan esterase, are required to completely hydrolyze mannans (34). Extremely thermophilic bacteria and hyperthermophilic archaea are known to produce several types of thermostable glycosyl hydrolases (38). Few thermostable ␤-mannanases from thermophilic bacteria have been characterized and sequenced (14,(17)(18)(19)33), while no archaeal ␤-mannanase has been described so far. The mannanases that have been sequenced belong to either glycosyl hydrolase family 5 or glycosyl hydrolase family 26 (22).Huang et al. (X. P. Huang, J. A. Hudson, F. A. Rainey, P. D. Nichols, and H. W. Morgan, submitted for publication) described a new thermophilic, spore-forming, aerobic bacterium related to the bacilli that was able to grow on crystalline cellulose, and they named this organism Caldibacillus cellulovorans. Their isolate was related to members of the genus Al...

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“…In contrast, two or more genes classified as members of the GH74 family in the CAZy database are present in many bacteria. Streptomyces species are the most extensively studied of these bacteria and have been used as a source of hemicellulases (2,4,9,12,19,20,23,28,32). Streptomyces avermitilis possesses two GH74 genes, which are similar to those found in Geotrichum sp.…”

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confidence: 83%

Characterization of an Endo-Processive-Type Xyloglucanase Having a β-1,4-Glucan-Binding Module and an Endo-Type Xyloglucanase from Streptomyces avermitilis

Ichinose

Araki

Michikawa

et al. 2012

Appl Environ Microbiol

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e We cloned two glycoside hydrolase family 74 genes, the sav_1856 gene and the sav_2574 gene, from Streptomyces avermitilis NBRC14893 and characterized the resultant recombinant proteins. The sav_1856 gene product (SaGH74A) consisted of a catalytic domain and a family 2 carbohydrate-binding module at the C terminus, while the sav_2574 gene product (SaGH74B) consisted of only a catalytic domain. SaGH74A and SaGH74B were expressed successfully and had molecular masses of 92 and 78 kDa, respectively. Both recombinant proteins were xyloglucanases. SaGH74A had optimal activity at 60°C and pH 5.5, while SaGH74B had optimal activity at 55°C and pH 6.0. SaGH74A was stable over a broad pH range (pH 4.5 to 9.0), whereas SaGH74B was stable over a relatively narrow pH range (pH 6.0 to 6.5). Analysis of the hydrolysis products of tamarind xyloglucan and xyloglucan-derived oligosaccharides indicated that SaGH74A was endo-processive, while SaGH74B was a typical endo-enzyme. The C terminus of SaGH74A, which was annotated as a carbohydrate-binding module, bound to ␤-1,4-linked glucan-containing soluble polysaccharides such as hydroxyethyl cellulose, barley glucan, and xyloglucan.

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ʲ-mannanase of Streptomyces lividans 66: cloning and DNA sequence of the manA gene and characterization of the enzyme

Cited by 87 publications

References 22 publications

Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β‐mannanase gene

Cloning and expression in Pichia pastoris of a blue mussel (Mytilus edulis) β‐mannanase gene

A Gene Encoding a Novel Multidomain β-1,4-Mannanase from Caldibacillus cellulovorans and Action of the Recombinant Enzyme on Kraft Pulp

Characterization of an Endo-Processive-Type Xyloglucanase Having a β-1,4-Glucan-Binding Module and an Endo-Type Xyloglucanase from Streptomyces avermitilis

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