Production and characterization of a new cyclodextrin glycosyltransferase from Bacillus firmus isolated from Brazilian soil

Moriwaki, Cristiane; Costa, Glauciane L.; Pazzetto, Rúbia; Zanin, Gisella Maria; Moraes, Flávio Faria de; Portilho, Márcia; Matioli, Graciette

doi:10.1016/j.procbio.2007.07.007

Cited by 31 publications

(21 citation statements)

References 23 publications

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“…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. G1 isolated by our group [28].…”

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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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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“…CGTase is an extracellular enzyme, and is a member of the amylolytic glycosylases family [9]. These are produced by Thermoanaerobacter [10] and by some species of Bacillus, such as Bacillus circulans [4], Bacillus macerans [11], Bacillus stearothermophilus [12], Bacillus agaradhaerens [13], and Bacillus firmus [14]. Alkalophilic bacilli have attracted much attention for industrial applications because of their high level of activity in wide pH and temperature ranges.…”

Section: Introductionmentioning

confidence: 99%

Cyclodextrin production by Bacillus firmus strain 37 immobilized on inorganic matrices and alginate gel

Mazzer

Ferreira

Rodella

et al. 2008

Biochemical Engineering Journal

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“…Until now there have been several reports on factors affecting CD production by CGTases from various microorganisms (Kim et al 1995;Charoenlap et al 2004;Szerman et al 2007). Some reports studied on the kinetics of CGTase but most of them focused only on the effect of substrate concentration (Gawande and Patkar, 2001;Matioli et al 2002;Arya and Srivastava, 2006;Moriwaki et al 2007). …”

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confidence: 99%

Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

Cheirsilp

Kitcha

Maneerat

2010

Electron. J. Biotechnol.

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The kinetic characteristics of β-cyclodextrin production by a cyclodextrin glycosyltransferase (CGTase) produced by Bacillus sp. C26, a new isolate from a soil sample was investigated. Considering highest yield and initial production rate of β-cyclodextrin, among the starches examined, soluble starch, tapioca starch, sago starch, corn starch and rice starch, tapioca starch was the best substrate for this CGTase. The optimum temperature for tapioca starch gelatinization prior to its use as a substrate for β-cyclodextrin production was 65ºC. The yield and initial production rate of β-cyclodextrin increased with increasing starch concentration up to 6% and an enzyme concentration up to 48 U/g-starch. The kinetic parameters of V max and K m of β-cyclodextrin production from tapioca starch by CGTase were 1.59 mg/mL/h and 22.3 mg/mL, respectively. Considering high initial production rate and high yield of β-cyclodextrin, the optimum reaction temperature was at 50ºC. This study provided the necessary kinetic information that may be useful to define the most suitable condition for industrialized production of β-cyclodextrin with the high yield and productivity.

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Production and characterization of a new cyclodextrin glycosyltransferase from Bacillus firmus isolated from Brazilian soil

Cited by 31 publications

References 23 publications

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

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

Cyclodextrin production by Bacillus firmus strain 37 immobilized on inorganic matrices and alginate gel

Kinetic characteristics of β-cyclodextrin production by cyclodextrin glycosyltransferase from newly isolated Bacillus sp. C26

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