Cloning and expression of the Bacillus subtilis No. 313 .GAMMA.-cyclodextrin forming CGTase gene in Escherichia coli.

Kato, Takashi; Horikoshi, Koki

doi:10.1271/bbb1961.50.2161

Cited by 11 publications

(5 citation statements)

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“…Cyclodextrin glucanotransferase (CGTase) is a unique type of α ‐ amylase which produces cyclodextrins (CDs) from starch, besides degrading starch to maltooligosaccharides. Several bacterial CGTases have been purified, and their genes have been cloned and characterized [1–8], including one from an alkalophilic bacterium, Bacillus ohbensis C‐1400 [9]. In our preliminary experiment, extracellular production of CGTase by B. ohbensis was detected only when the cells were grown in the presence of starch.…”

Section: Introductionmentioning

confidence: 87%

Regulation of cyclodextrin glucanotransferase synthesis in Bacillus ohbensis

Nishida

Nakamura

Hara

et al. 2006

FEMS Microbiology Letters

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The production of cyclodextrin glucanotransferase (CGTase) by Bacillus ohbensis is dependent on the presence of starch and inhibited by glucose in the medium. Northern blot analysis revealed that the CGTase gene (cgt) was transcribed to almost the same level irrespective of the presence or absence of starch, but glucose completely repressed the transcription. Furthermore, a relatively high amount of CGTase protein was detected on Western blotting only in the medium with starch, showing the lack of posttranslational control of the CGTase activity. These findings suggest some starch induction mechanism for the cgt gene, possibly at the posttranscriptional level, besides negative transcriptional regulation by glucose.

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Section: Introductionmentioning

confidence: 87%

Regulation of cyclodextrin glucanotransferase synthesis in Bacillus ohbensis

Nishida

Nakamura

Hara

et al. 2006

FEMS Microbiology Letters

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“…CDs are highly valuable modified starches that are extensively used as molecular chelating agents in the cosmetic, pharmaceutical, food, agricultural, and chemical industries [24]. In 1986, the recombinant production of a Bacillus CGTase in E. coli was carried out by Kato and Horikoshi [14]. Since then, many CGTase genes have been isolated and expressed in E. coli [16,26], including a b-CGTase from Bacillus sp.…”

Section: Introductionmentioning

confidence: 99%

An effective extracellular protein secretion by an ABC transporter system in Escherichia coli: statistical modeling and optimization of cyclodextrin glucanotransferase secretory production

Low¹,

Mahadi²,

Rahim³

et al. 2011

J Ind Microbiol Biotechnol

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Direct transport of recombinant protein from cytosol to extracellular medium offers great advantages, such as high specific activity and a simple purification step. This work presents an investigation on the potential of an ABC (ATP-binding cassette) transporter system, the hemolysin transport system, for efficient protein secretion in Escherichia coli (E. coli). A higher secretory production of recombinant cyclodextrin glucanotransferase (CGTase) was achieved by a new plasmid design and subsequently by optimization of culture conditions via central composite design. An improvement of at least fourfold extracellular recombinant CGTase was obtained using the new plasmid design. The optimization process consisted of 20 experiments involving six star points and six replicates at the central point. The predicted optimum culture conditions for maximum recombinant CGTase secretion were found to be 25.76 μM IPTG, 1.0% (w/v) arabinose and 34.7°C post-induction temperature, with a predicted extracellular CGTase activity of 68.76 U/ml. Validation of the model gave an extracellular CGTase activity of 69.15 ± 0.71 U/ml, resulting in a 3.45-fold increase compared to the initial conditions. This corresponded to an extracellular CGTase yield of about 0.58 mg/l. We showed that a synergistic balance of transported protein and secretory pathway is important for efficient protein transport. In addition, we also demonstrated the first successful removal of the C-terminal secretion signal from the transported fusion protein by thrombin proteolytic cleavage.

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“…Another reason for the crucial role of the enzyme is that at a higher enzymic concentration, a higher yield is obtained. Naturally therefore, many industry-affiliated research laboratories have lately offered large resources for genetic manipulation of the CGTase-excreting bacteria (Binder et al 1986, Kato and Horikoshi 1986a, Takano et al 1986, Kimura et al 1987 . No report on overproducing CGTase-strain has been published thus far although such might be expected quite soon.…”

Section: Production Of the Enzymementioning

confidence: 99%

Cyclodextrins: Production, properties and applications in food chemistry

et al. 1988

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Cyclodextrins have diverse, important applications in food industry. These applications are based on the ability of cyclodextrins to form molecular complexes with small-molecular compounds. Cyclodextrins are harmless in oral administration and advantageous effects by cyclodextrins are achieved by simple mixing of small amounts of them to the material being stabilized. Development of convenient and cost-effective processes for production of cyclodextrins are undergoing and there are promises in the near future for obtaining cyclodextrins which are realistic in price to be used in foods. While cyclodextrins have been used for more than ten years in Japan as natural additives in foods, the legislation for their approval in foods is still under development in Europe and USA.

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Cloning and expression of the Bacillus subtilis No. 313 .GAMMA.-cyclodextrin forming CGTase gene in Escherichia coli.

Cited by 11 publications

References 1 publication

Regulation of cyclodextrin glucanotransferase synthesis in Bacillus ohbensis

Regulation of cyclodextrin glucanotransferase synthesis in Bacillus ohbensis

An effective extracellular protein secretion by an ABC transporter system in Escherichia coli: statistical modeling and optimization of cyclodextrin glucanotransferase secretory production

Cyclodextrins: Production, properties and applications in food chemistry

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