Additional Carbohydrate-Binding Modules Enhance the Insoluble Substrate-Hydrolytic Activity of β-1,3-Glucanase from Alkaliphilic<i>Nocardiopsis</i>sp. F96

Koizumi, Naoya; Masuda, Sumiko; Maeda, K.; Isoda, Yuya; Yatsunami, Rie; Fukui, Toshiaki

doi:10.1271/bbb.80846

Cited by 7 publications

(3 citation statements)

References 32 publications

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“…This thermostable enzyme could be put to use for preparing high-fructose syrups. Such syrups are extensively preferred β-1,3-1,4-glucans rather than β-1,3-glucans; cloning and expression; crystal structure; construction and characterization of chimeras Masuda et al 2003Masuda et al , 2006Fibriansah et al 2006Fibriansah et al , 2007Koizumi et al 2007Koizumi et al , 2009 Alkali-tolerant thermostable inulinase Xylan bioconversion into xylose for different products Tsujibo et al 1990aTsujibo et al , 1991 used in the beverage industry as sweeteners for making soft drinks (Van der Maarel et al 2002). Another recent paper describes the isolation and immobilization of a thermostable α-amylase derived from a haloalkaliphilic marine isolate referred to as Nocardiopsis sp.…”

Section: Carbohydrases Obtained From Nocardiopsis Speciesmentioning

confidence: 99%

“…In order to enhance the enzymatic properties of BglF, additional carbohydrate-binding domains were introduced, chimera proteins were created, and they were characterized (Koizumi et al , 2009. Four chimeras containing BglF along with the following carbohydrate-binding modules (i) Cterminal additional domain (CAD) of β-1,3-glucanase H from Bacillus circulans IAM1165, (ii) N-terminal additional domain (NAD) of β-1,3-glucanase H from B. circulans IAM1165, (iii) both CAD and NAD and (iv) chitin-binding domain (ChBD) of chitinase from alkaliphilic Bacillus sp.…”

Section: Carbohydrases Obtained From Nocardiopsis Speciesmentioning

confidence: 99%

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Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Bennur

Kumar

Zinjarde

et al. 2014

Appl Microbiol Biotechnol

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Members of the genus Nocardiopsis are generally encountered in locations that are inherently extreme. They are present in frozen soils, desert sand, compost, saline or hypersaline habitats (marine systems, salterns and soils) and alkaline places (slag dumps, lake soils and sediments). In order to survive under these severe conditions, they produce novel and diverse enzymes that allow them to utilize the available nutrients and to thrive. The members of this genus are multifaceted and release an assortment of extracellular hydrolytic enzymes. They produce enzymes that are cold-adapted (α-amylases), thermotolerant (α-amylases and xylanases), thermoalkalotolerant (cellulases, β-1,3-glucanases), alkali-tolerant thermostable (inulinases), acid-stable (keratinase) and alkalophilic (serine proteases). Some of the enzymes derived from Nocardiopsis species act on insoluble polymers such as glucans (pachyman and curdlan), keratin (feathers and prion proteins) and polyhydroxyalkanoates. Extreme tolerance exhibited by proteases has been attributed to the presence of some amino acids (Asn and Pro) in loop structures, relocation of multiple salt bridges to outer regions of the protein or the presence of a distinct polyproline II helix. The range of novel enzymes is projected to increase in the forthcoming years, as new isolates are being continually reported, and the development of processes involving such enzymes is envisaged in the future.

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Section: Carbohydrases Obtained From Nocardiopsis Speciesmentioning

confidence: 99%

Section: Carbohydrases Obtained From Nocardiopsis Speciesmentioning

confidence: 99%

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Bennur

Kumar

Zinjarde

et al. 2014

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

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“…Even high sequence similarity was found between PglA and the β-1,3-glucanase BglH from Bacillus circulans IAM1165, PglA possessed a novel Ig-like domain which was not observed in BglH by conserved domain search in NCBI. Previous reports demonstrated carbohydrate-binding properties of the N-and C-terminal regions of BglH [27,32], while, the effects of the non-catalytic domain on enzymatic properties of BglH were not described. Furthermore, the enzymatic properties of Ig-like domain, which is generally considered being involved in carbohydrate binding and commonly found in bacterial proteins [33], have not been illustrated in bacterial β-1,3-glucanases.…”

Section: Discussionmentioning

confidence: 99%

Recombinant production and characterization of full-length and truncated β-1,3-glucanase PglA from Paenibacillussp. S09

Cheng

Chen

et al. 2013

BMC Biotechnol

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Backgroundβ-1,3-Glucanases catalyze the hydrolysis of glucan polymers containing β-1,3-linkages. These enzymes are of great biotechnological, agricultural and industrial interest. The applications of β-1,3-glucanases is well established in fungal disease biocontrol, yeast extract production and wine extract clarification. Thus, the identification and characterization of novel β-1,3-glucanases with high catalytic efficiency and stability is of particular interest.ResultsA β-1,3-glucanase gene designated PglA was cloned from a newly isolated strain Paenibacillus sp. S09. The gene PglA contained a 2631-bp open reading frame encoding a polypeptide of 876 amino acids which shows 76% identity with the β-1,3-glucanase (BglH) from Bacillus circulans IAM1165. The encoded protein PglA is composed of a signal peptide, an N-terminal leader region, a glycoside hydrolase family 16 (GH16) catalytic domain and a C-terminal immunoglobulin like (Ig-like) domain. The Escherichia coli expression system of PglA and five truncated derivatives containing one or two modules was constructed to investigate the role of catalytic and non-catalytic modules. The pH for optimal activity of the enzymes was slightly affected (pH 5.5-6.5) by the presence of different modules. However, the temperature for optimal activity was strongly influenced by the C-terminal domain and ranged from 50 to 60°C. Deletion of C-terminal domain resulted in obviously enhancing enzymatic thermostability. Specific activity assay indicated that PglA specifically hydrolyzes β-1,3-glucan. Insoluble β-1,3-glucan binding and hydrolysis were boosted by the presence of N-and C-terminal domains. Kinetic analysis showed that the presence of N-and C-terminus enhances the substrate affinity and catalytic efficiency of the catalytic domain toward laminarin. Carbohydrate-binding assay directly confirmed the binding capabilities of the N-and C-terminal domains.ConclusionsThis study provides new insight into the impacts of non-catalytic modules on enzymatic properties of β-1,3-glucanase. Activity comparison of full-length PglA and truncated forms revealed the negative effect of C-terminal region on thermal stability of the enzyme. Both the N-and C-terminal domains exerted strong binding activity toward insoluble β-1,3-glucan, and could be classified into CBM families.

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Aromatic residues in N-terminal domain of archaeal trehalase affect the folding and activity of catalytic domain

Sakoh,

Satoh,

Domon

et al. 2024

Appl Microbiol Biotechnol

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Additional Carbohydrate-Binding Modules Enhance the Insoluble Substrate-Hydrolytic Activity of β-1,3-Glucanase from AlkaliphilicNocardiopsissp. F96

Cited by 7 publications

References 32 publications

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Nocardiopsis species as potential sources of diverse and novel extracellular enzymes

Recombinant production and characterization of full-length and truncated β-1,3-glucanase PglA from Paenibacillussp. S09

Aromatic residues in N-terminal domain of archaeal trehalase affect the folding and activity of catalytic domain

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