Optimization of Cyclodextrin Glycosyltransferase Production from <i>Klebsiella</i><i>pneumoniae</i>AS‐22 in Batch, Fed‐Batch, and Continuous Cultures

Gawande, Bharat; Sonawane, Avinash; Jogdand, Vithal V.; Patkar, Anant

doi:10.1021/bp034115t

Cited by 23 publications

(18 citation statements)

References 16 publications

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“…CGTase also exhibits weak hydrolyzing activity (Tonkova 1998). CGTase is produced mainly from a variety of Bacillus species (Tonkova 1998) and Klebsiella pneumoniae (Gawande et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Production of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. by pH-stat fed-batch fermentation

et al. 2009

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Batch and fed-batch fermentation processes were employed to culture an alkalophilic Bacillus sp. for the production of cyclodextrin glucanotransferase (CGTase). CGTase production was repressed by glucose and induced by soluble starch. By fed-batch fermentation, a CGTase activity up to 56 unit ml(-1) with 65 g dry cells l(-1) were achieved. The CGTase activity and cell density were increased 360 and 510%, respectively, from those values achieved with batch fermentation.

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“…CGTase also exhibits weak hydrolyzing activity (Tonkova 1998). CGTase is produced mainly from a variety of Bacillus species (Tonkova 1998) and Klebsiella pneumoniae (Gawande et al 2003).…”

Section: Introductionmentioning

confidence: 99%

Production of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. by pH-stat fed-batch fermentation

et al. 2009

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“…The starch iodine complex formation was quantified by measuring absorbance at 700 nm. One unit of enzyme activity was defined as the amount that elicited a 10% reduction in absorbance (Gawande et al 2003). In the formula below, 'a' is the optical density (OD/min) of the reaction from the control group, and 'b' is the OD of the reaction from the sample.…”

Section: Enzyme Activity Assaysmentioning

confidence: 99%

Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues

Wang

Zhou

et al. 2017

3 Biotech

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b-Cyclodextrin glycosyltransferase (b-CGTase) belongs to the a-amylase family of enzymes and converts starch to cyclic oligosaccharides called b-cyclodextrins (b-CD). The b-CGTase from alkalophilic Bacillus sp. N-227 was separately mutagenized to give three site-directed bCGTase mutants, Y127F, R254F and D355R, that showed enhanced cyclization activity towards a starch substrate from 1.64 to 2.1-folds. Kinetic studies indicate that the mutants had higher affinity towards the substrate than the wild type b-CGTase. The Y127F mutant had the highest affinity which was indicated by the lowest K m of 15.30 mM and the highest catalytic activity. Increasing hydrophobicity around the catalytic center appeared to favor the cyclization activity of the mutants. The bCGTase and the three mutants showed optimal enzyme activity at 60°C and pH 6.0. All the enzymes were stable for at least 60 min across a wide pH range (5.0-7.0).

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“…Moreover, high concentrations of starch increase the viscosity of the medium and lead to catabolite repression. [6,38] Therefore, the optimal concentration of carbon source obtained seems to be suitable in order to improve the CGTase production and at the same time to prevent the catabolite repression, high viscosity and extensive growth inhibition. Menocci and Goulart [21] conducted a study on carbon source optimization for CGTase production by Bacillus sp.…”

Section: Artificial Neural Networkmentioning

confidence: 99%

Cyclodextrin glycosyltransferase biosynthesis improvement by recombinantLactococcus lactisNZ:NSP:CGT: medium formulation and culture condition optimization

Amiri

Mohamad

Rahim

et al. 2015

Biotechnology & Biotechnological Equipment

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Cyclodextrin glycosyltransferase (CGTase) is a bacterial glycosyltransferase which catalyses the conversion of starch to cyclodextrin. It can be produced industrially through a fermentation process. The optimal design of the fermentation medium and conditions is critical for metabolic production and microbial growth. Optimization of CGTase biosynthesis by recombinant Lactococcus lactis NZ:NSP:CGT was performed using an artificial neural network (ANN) as the main tool in order to improve the CGTase production in the fermentation process. Three parameters, including temperature, carbon source concentration and nitrogen source concentration, were determined as significant factors for improvement of CGTase production by L. lactis NZ:NSP:CGT in the fermentation process. Soluble potato starch and yeast extract were chosen as the best carbon and nitrogen sources for higher production of CGTase by L. lactis NZ:NSP:CGT. The optimum concentration of soluble starch and yeast extract were 3.82% and 5.67% (w/v), respectively, and the optimum temperature was 20C. The final CGTase activity under optimized conditions was 22.09 U/mL, which was close enough to the predicted value of 24.17 U/mL. The obtained results are of particular interest, as CGTase is an industrially important enzyme. In this study, its production through batch fermentation was optimized in order to maximize its production. In future studies, more investigations in various modes of fermentation should be conducted in order to increase the CGTase biosynthesis.

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Optimization of Cyclodextrin Glycosyltransferase Production from KlebsiellapneumoniaeAS‐22 in Batch, Fed‐Batch, and Continuous Cultures

Cited by 23 publications

References 16 publications

Production of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. by pH-stat fed-batch fermentation

Production of cyclodextrin glucanotransferase from an alkalophilic Bacillus sp. by pH-stat fed-batch fermentation

Improved activity of β-cyclodextrin glycosyltransferase from Bacillus sp. N-227 via mutagenesis of the conserved residues

Cyclodextrin glycosyltransferase biosynthesis improvement by recombinantLactococcus lactisNZ:NSP:CGT: medium formulation and culture condition optimization

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