A novel cyclodextrin glycosyltransferase from Bacillus sphaericus strain 41: Production, characterization and catalytic properties

Moriwaki, Cristiane; Ferreira, Lívia Rosas; Rodella, Júlia Regina Tedesco; Matioli, Graciette

doi:10.1016/j.bej.2009.09.001

Cited by 47 publications

(33 citation statements)

References 34 publications

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“…However, low cyclization activities have also been reported for CGTases from thermophilic Thermoanaerobacter sp. P4 (Avci and Donmez, 2009), Bacillus agaradhaerens LS-3C (Martins and Hatti-Kaul, 2003) and Bacillus sphaericus (Moriwaki et al, 2009). As shown in Figure 1, within 12 h of fermentation, the amount of CGTase production was very small and could hardly be detected.…”

Section: Sk13002mentioning

confidence: 86%

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Sun¹,

Letsididi²,

Pan³

2013

Afr. J. Microbiol. Res.

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A β-cyclodextrin glycosyltransferase (β-CGTase) from a new alkalitolerant Bacillus sp. SK 13.002 strain which can significantly hydrolyze starch into short linear saccharides, in addition to production of cyclodextrins (CDs) was produced. The hydrolytic activity of this CGTase as a side reaction is thought to be due to partial retention of ancestral enzyme function from evolution over time. This CGTase is therefore another example of an enzyme at an intermediary stage in between ''true'' α-amylases and ''true'' CGTases. The strain also produced two CGTase isozymes which were purified to homogeneity using DEAE-Sepharose anion exchange chromatography and Superdex 75 gel filtration chromatography to show Molecular masses of 67.5 and 46.8 kDa on sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) respectively, which were confirmed by liquid chromatography/mass spectrometry (LC/MS) analysis to be 67.6 and 47.3 kDa, respectively. Both CGTase isozymes formed CDs from soluble starch. Most of the reported CGTases were composed of one single enzyme with only a few strains having CGTase isozymes showing different isoelectric points. Therefore, Bacillus sp. SK 13.002 strain is another Bacillus capable of producing CGTase isozymes which were individually purified to homogeneity.

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Section: Sk13002mentioning

confidence: 86%

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Sun¹,

Letsididi²,

Pan³

2013

Afr. J. Microbiol. Res.

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“…On the other hand, industrial production of enzyme with freecell continuous process fermentation is not usually adequate [36]. Moriwaki [4] studied batch CGTase production using Bacillus sphaericus strain 41 and achieved a maximum enzyme activity of 0.048 U/mL at 120 hours. All these comparisons indicate that there are several factors interfering in enzyme production.…”

Section: Resultsmentioning

confidence: 99%

“…The CGTase is considered a multifunctional enzyme, catalyzing four reactions: cyclization (intramolecular transglycosylation reaction), coupling (intermolecular transglycosylation reaction, wherein the cyclodextrin ring is ruptured and transferred to straight acceptors), disproportionation (where two linear oligosaccharides are converted into linear oligosaccharides of different sizes) and starch hydrolysis [4]. These reactions can be performed in a wide range of pH and temperatures, thus expanding the possibilities for industrial applications of CGTase [3].…”

Section: Introductionmentioning

confidence: 99%

Bovine Bone Charcoal as Support Material for Immobilization of <em>Bacillus firmus</em> Strain 37 and Production of Cyclomaltodextrin Glucanotransferase by Batch Fermentation in a Fluidized Bed

Silva¹,

Bieli²,

Valarini³

et al. 2018

ACES

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The process described in the present work uses air supplementation in a fluidized bed reactor containing Bacillus firmus strain 37 immobilized on active bovine bone charcoal, to produce by batch fermentation the enzyme CGTase (cyclomaltodextrin-glucanotransferase). Three different aeration rates were evaluated. The maximum CGTase activity was achieved after 120 hours of fermentation with aeration rate of 2 vvm and was equal to 2.48 U/mL. When 0.5 and 1 vvm were used the enzymatic activities achieved 1.1 and 0.57 U/mL, respectively. Bovine bone charcoal was characterized in terms of surface area, pore size and volume. To the best of our knowledge, the immobilization of microorganism cells in bovine bone charcoal for CGTase production has not been reported in the literature. Our results showed that fluidized bed reactor allows retaining high concentration of biomass, improving biomass-substrate contact and operation at low residence times, which resulted in improved enzyme production. Therefore, the process as proposed has great potential for industrial development.

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“…Mahat et al (2004) pointed out that the yeast extract concentration in the media is a major significant factor for the CGTase production. Furthermore, the presence of essential nutrients or inductors can stimulate the production of the enzyme (Moriwaki et al 2009). …”

Section: Resultsmentioning

confidence: 99%

Improvement of cyclodextrin glycosyltransferase (CGTase) production by recombinant Escherichia coli pAD26 immobilized on the cotton

et al. 2012

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Abstract:The cyclodextrin glycosyltransferase (CGTase) of the recombinants Escherichia coli pAD26 cells immobilized on cotton was optimally produced by statistical methodology. Primarily, carbon and nitrogen sources were selected by one-factor-at-a-time method. Wheat starch, Casamino acid, Edamin and Hy-soy were identified as the best nutrients. These sources were secondly confirmed by Plackett-Burman design (fifteen variables were studied with sixteen experiments), as the most significant components with respect to CGTase production. In the third step, concentration of most significant factors and their interaction were optimized with a Box-Behnken experimental design. Under the optimized conditions (agitation 200 rpm, yeast extract concentration 20 g/L, wheat starch concentration 10 g/L and Hy-soy concentration 2.5 g/L), CGTase yield 145.11 U/mL was 3.6 and 23 folds higher than those obtained by the use of the initial conditions (39.77 U/mL) and free cells (6.37 U/mL), respectively.

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A novel cyclodextrin glycosyltransferase from Bacillus sphaericus strain 41: Production, characterization and catalytic properties

Cited by 47 publications

References 34 publications

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Bovine Bone Charcoal as Support Material for Immobilization of <em>Bacillus firmus</em> Strain 37 and Production of Cyclomaltodextrin Glucanotransferase by Batch Fermentation in a Fluidized Bed

Improvement of cyclodextrin glycosyltransferase (CGTase) production by recombinant Escherichia coli pAD26 immobilized on the cotton

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A novel cyclodextrin glycosyltransferase from Bacillus sphaericus strain 41: Production, characterization and catalytic properties

Cited by 47 publications

References 34 publications

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Production of a novel Cyclodextrin glycosyltransferase from Bacillus sp. SK13.002

Bovine Bone Charcoal as Support Material for Immobilization of &lt;em&gt;Bacillus firmus&lt;/em&gt; Strain 37 and Production of Cyclomaltodextrin Glucanotransferase by Batch Fermentation in a Fluidized Bed

Improvement of cyclodextrin glycosyltransferase (CGTase) production by recombinant Escherichia coli pAD26 immobilized on the cotton

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Product

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Bovine Bone Charcoal as Support Material for Immobilization of <em>Bacillus firmus</em> Strain 37 and Production of Cyclomaltodextrin Glucanotransferase by Batch Fermentation in a Fluidized Bed