A novel thermophilic anaerobic bacteria producing cyclodextrin glycosyltransferase

Avcı, Ayşe; Dönmez, Sedat

doi:10.1016/j.procbio.2008.09.006

Cited by 27 publications

(21 citation statements)

References 38 publications

(45 reference statements)

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“…2). According to Avci & Dönmez (2009), casein is the best nitrogen source for the CGTase production. Edamin and Hy-soy also showed significant CGTase production with the 26.35 U/mL and the 26.13 U/mL respectively.…”

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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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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“…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: 98%

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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“…P4 is thermophilic anaerobic bacterium which produces CGTase. It was identified and CGTase production conditions were determined in our previous study (Avci and Donmez, 2009). In this work, purification results and some properties of the purified CGTase from Thermoanaerobacter sp.…”

Section: Introductionmentioning

confidence: 93%

“…P4 according to 16S rRNA studies and biochemical characteristics (Avci and Donmez, 2009). DSMZ medium no 144 was used for the growth of bacteria (www.dsmz.de/mediumlist).…”

Section: Bacterial Strainmentioning

confidence: 99%

Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4

Avcı¹,

Dönmez²

2012

Afr. J. Biotechnol.

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Cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) from a thermophilic anaerobic bacterium, Thermoanaerobacter sp. P4, was purified by ammonium sulfate precipitation followed by α-cyclodextrin epoxy activated-sepharose 6B column chromatography. Enzyme was purified 141 fold and had the specific activity of 143.8 U/mg proteins. Purification yields after ammonium sulfate precipitation and affinity chromatography were 25.8 and 17.8%, respectively. SDS-PAGE analysis showed that enzyme was purified successfully and had a single band. Molecular weight of the enzyme was determined as 68.7 kDa. The enzyme had optimum cyclization activity at 80 to 90°C and hydrolyzing activity at 90°C and maintained 87 and 95% of these activities at 95°C, respectively. Optimal pH was found as 7.0. It retained full activity at 80°C for 4 h. Enzyme was strongly inhibited by HgSO 4 and AgNO 3 . Addition of 1 mM CaCl 2 increased the enzymatic activity up to 7%. This novel enzyme could be a good candidate for industrial applications according to its characteristic found in the current study.

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A novel thermophilic anaerobic bacteria producing cyclodextrin glycosyltransferase

Cited by 27 publications

References 38 publications

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

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

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

Purification and characterization of a thermostable cyclodextrin glycosyltransferase from Thermoanaerobacter sp. P4

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