Effects of immobilization, pH and reaction time in the modulation of α-, β- or γ-cyclodextrins production by cyclodextrin glycosyltransferase: Batch and continuous process

Schöffer, Jéssie da Natividade; Matte, Carla Roberta; Charqueiro, Douglas Santana; Menezes, Eliana Weber de; Costa, Tânia Maria Haas; Benvenutti, Edílson V.; Rodrigues, Rafael C.; Hertz, Plinho Francisco

doi:10.1016/j.carbpol.2017.04.005

Cited by 19 publications

(5 citation statements)

References 58 publications

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“…The CD increment occurred when the reaction time was increased due to the frequent binding between tapioca starch and enzyme, thus improved the reaction process for the production of CD (Ibrahim, 2013). The results from Schöffer et al (2017) was similar with the findings from the present study on the production of CD using CGTase from Thermoanaerobacter sp. Reduction in the concentration of CD was observed when increasing the reaction time for reaction process.…”

Section: Substrate Concentration (%)supporting

confidence: 91%

Effect of Reaction Parameters on the Production of Cyclodextrin using Cyclodextrin Glucanotransferase from Bacillus licheniformis

Man

Shaarani@Nawi

Arshad

et al. 2020

JCEIB

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Cyclodextrin glucanotransferase (CGTase) is an industrial enzyme that converts starch into cyclodextrin (CD). CD has many potential applications in wide range of industries including food, cosmetic, pharmaceutical and plastic industries. Production of CD from CGTase is based on a few process parameters such as concentration of substrate, types of substrate, reaction time, pH and temperature. In this present study, the effect of types of substrate (corn, potato, wheat, rice and tapioca starch), concentration of substrate (1, 2, 3, 4, 5, 6, 7, 8 and 9%) and reaction time (1, 2, 3, 4 and 5 hr) on the CD production using commercial CGTase from Bacillus licheniformis were studied. Among the five types of substrate tested, the potato starch was the most suitable substrate for the production of CD with 10.24 mg/ml of CD. In addition, by using 6% (w/v) of potato starch, the production of CD was 15.16 mg/ml. The optimal reaction time was found to be 4 hr with 12.41 mg/ml of CD. Therefore, the best reaction parameters proved to be valuable for the highest CD production. Hence, CGTase from Bacillus licheniformis was demonstrated to produce high CD at optimum reaction conditions and it has potential to be used in large scale production for the industrial purposes.

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Section: Substrate Concentration (%)supporting

confidence: 91%

Effect of Reaction Parameters on the Production of Cyclodextrin using Cyclodextrin Glucanotransferase from Bacillus licheniformis

Man

Shaarani@Nawi

Arshad

et al. 2020

JCEIB

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“…It was shown that increase in surface hydrophobicity led to higher adsorbed protein [ 32,36 ] due to a decreased effect of competitive interactions with water molecules. [ 37 ]…”

Section: Resultsmentioning

confidence: 99%

“…It was shown that increase in surface hydrophobicity led to higher adsorbed protein [32,36] due to a decreased effect of competitive interactions with water molecules. [37] Although, GNP had better uptake of CGTase, its lower residual activity compared to Ca-TMA could be attributed to the larger changes in secondary structures, as discussed in Section 3.2. Also, it is possible that some of the CGTase could be attached within the stacks of graphene layer or its micropores, thus, reducing the active sites available for starch degradation.…”

Section: Cgtase Immobilizationmentioning

confidence: 98%

Immobilization of Cyclodextrin glycosyltransferase onto three dimensional‐ hydrophobic and two dimensional‐ hydrophilic supports: A comparative study

Ogunbadejo,

Aljahoushi,

Alzamly

et al. 2023

Biotechnology Journal

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Cyclodextrin glycosyltransferase (CGTase) degrades starch into cyclodextrin via enzymatic activity. In this study, we immobilize CGTase from Thermoanaerobacter sp. on two supports, namely graphene nanoplatelets (GNP) consisting of short stacks of graphene nanoparticles and a calcium‐based two‐dimensional metal organic framework (Ca‐TMA). The uptakes of CGTase on GNP and Ca‐TMA reached 40 and 21 mg g−1 respectively, but immobilized CGTase on Ca‐TMA showed a higher specific activity (38 U mg−1) than that on GNP (28 U mg−1). Analysis of secondary structures of CGTase, shows that immobilization reduces the proportion of β‐sheets in CGTase from 56% in the free to 49% and 51.3% for GNP and Ca‐TMA respectively, α‐helix from 38.5% to 18.1 and 37.5%, but led to increased β‐turns from 5.5 to 40% and 11.2% for GNP and Ca‐TMA, respectively. Lower levels of conformational changes were observed over the more hydrophilic Ca‐TMA compared to hydrophobic GNP, resulting in its better activity. Increased β‐turns were found to correlate with lower β‐CD production, while more β‐sheets and α‐helix favored more β‐CD. Reusability studies revealed that GNP retains up to 74% of initial CGTase activity, while Ca‐TMA dropped to 33% after eight consecutive uses. The results obtained in this work provide insight on the effect of support's surface properties on CGTase performance and can assist in developing robust CGTase‐based biocatalysts for industrial application.

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“…This finding can be attributed to the favorable interaction between the carrier and the enzyme, resulting in enzyme folding into the optimum conformation on the surface of the PHA granules, thus increasing the enzyme activity [ 21 , 23 ]. Furthermore, the γ-CGTase-PHA nanobiocatalyst was found to possess a considerable specific activity of 347.9 U/g beads (dry weight), considerably higher than that of other immobilized CGTases reported in most recent studies, such as glyoxyl–agarose immobilized CGTase (27.38 U/g support) [ 13 ], cellulose nanofiber immobilized CGTase (159.34 U/g support) [ 14 ], and glutaraldehyde pre-activated silica immobilized CGTase (101.73 U/g support) [ 35 ]. This finding is likely because PhaC dictates a homogenous orientation of its fusion partner on the nanobeads’ surface, hence providing a maximum interaction with substrates and increased accessibility to substrates, leading to high specific activity of the immobilized enzymes if properly engineered [ 22 , 36 ].…”

Section: Discussionmentioning

confidence: 96%

“…7 b) in the CDs produced by γ-CGTase-PHA beads was the highest among previously published immobilized CGTases, indicating that the difficulty and cost of subsequent separation and extraction of γ-CD could be greatly reduced. However, the yield (22.73%) of γ-CD was not the highest among the published immobilized CGTases; the γ-CD yield was lower than that obtained from immobilized β-CGTase on glutaraldehyde pre-activated silica (26% β-CD, pH 4.0, 70 °C) [ 35 ] and glyoxyl–agarose (29% β-CD, 85 °C) [ 13 ], but compared favorably with that of CGTases immobilized on other substances, such as aminated polyvinylchloride (PVC) (15.6%) [ 39 ] and resin (FE 4611) (14%) [ 12 ]. When the immobilized γ-CGTase level was further increased, the yield and the ratio of γ-CD at equilibrium were not further improved (Fig.…”

Section: Discussionmentioning

confidence: 99%

Economical synthesis of γ-cyclodextrin catalyzed by oriented cyclodextrin glycosyltransferase displayed on bacterial polyhydroxyalkanoate nanogranules

Duan,

Wang,

Tan

et al. 2023

Microb Cell Fact

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Background The advantages of γ-cyclodextrin (γ-CD) include its high solubility, ability to form inclusion complexes with various poorly water-soluble molecules, and favorable toxicological profile; thus, γ-CD is an attractive functional excipient widely used in many industrial settings. Unfortunately, the high cost of γ-CD caused by the low activity and stability of γ-cyclodextrin glycosyltransferase (γ-CGTase) has hampered large-scale production and application. Results This study reports the in vivo one-step production of immobilized γ-CGTase decorated on the surface of polyhydroxyalkanoate (PHA) nanogranules by the N-terminal fusion of γ-CGTase to PHA synthase via a designed linker. The immobilized γ-CGTase-PHA nanogranules showed outstanding cyclization activity of 61.25 ± 3.94 U/mg (γ-CGTase protein) and hydrolysis activity of 36,273.99 ± 1892.49 U/mg, 44.74% and 18.83% higher than that of free γ-CGTase, respectively. The nanogranules also exhibited wider optimal pH (cyclization activity 7.0–9.0, hydrolysis activity 10.0–11.0) and temperature (55–60 °C) ranges and remarkable thermo- and pH-stability, expanding its utility to adapt to wider and more severe reaction conditions than the free enzyme. A high yield of CDs (22.73%) converted from starch and a high ratio (90.86%) of γ-CD in the catalysate were achieved at pH 9.0 and 50 °C for 10 h with 1 mmol/L K+, Ca2+, and Mg2+ added to the reaction system. Moreover, γ-CGTase-PHA beads can be used at least eight times, retaining 82.04% of its initial hydrolysis activity and 75.73% of its initial cyclization activity. Conclusions This study provides a promising nanobiocatalyst for the cost-efficient production of γ-CD, which could greatly facilitate process control and economize the production cost.

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Effects of immobilization, pH and reaction time in the modulation of α-, β- or γ-cyclodextrins production by cyclodextrin glycosyltransferase: Batch and continuous process

Cited by 19 publications

References 58 publications

Effect of Reaction Parameters on the Production of Cyclodextrin using Cyclodextrin Glucanotransferase from Bacillus licheniformis

Effect of Reaction Parameters on the Production of Cyclodextrin using Cyclodextrin Glucanotransferase from Bacillus licheniformis

Immobilization of Cyclodextrin glycosyltransferase onto three dimensional‐ hydrophobic and two dimensional‐ hydrophilic supports: A comparative study

Economical synthesis of γ-cyclodextrin catalyzed by oriented cyclodextrin glycosyltransferase displayed on bacterial polyhydroxyalkanoate nanogranules

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