Production of γ-cyclodextrin by Bacillus cereus cyclodextrin glycosyltransferase using extractive bioconversion in polymer-salt aqueous two-phase system

Lin, Yu; Show, Pau Loke; Yap, Yee Jiun; Ariff, Arbakariya; Annuar, Mohammad Suffian Mohammad; Lai, Oi Ming; Tang, Teck Kim; Juan, Joon Ching; Ling, Tau Chuan

doi:10.1016/j.jbiosc.2015.11.001

Cited by 18 publications

(5 citation statements)

References 20 publications

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“…Therefore, it can be seen that to ensure the effectiveness and performance of bioconversion, the CGTase enzyme in the bottom phase should not be recycled more than once. One of our earlier studies about extractive bioconversion of γ-CD from soluble starch with CGTase enzyme by using PEG instead of EOPO (Lin et al, 2015 ). Table 3 shows the γ-CD concentration ratio within 2 h in the present study was lower than that within 1 h in our previous study (Lin et al, 2015 ).…”

Section: Resultsmentioning

confidence: 99%

“…One of our earlier studies about extractive bioconversion of γ-CD from soluble starch with CGTase enzyme by using PEG instead of EOPO (Lin et al, 2015 ). Table 3 shows the γ-CD concentration ratio within 2 h in the present study was lower than that within 1 h in our previous study (Lin et al, 2015 ). However, the LBS using EOPO is more economical and environmentally-friendly than that using PEG, as described in introduction.…”

Section: Resultsmentioning

confidence: 99%

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Extractive Bioconversion of Gamma-Cyclodextrin and Recycling of Cyclodextrin Glycosyltransferase in Liquid Biphasic System Using Thermo-Separating Polymer

et al. 2018

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An extractive bioconversion conducted on soluble starch with cyclodextrin glycosyltransferase (CGTase) enzyme in ethylene oxide-propylene oxide (EOPO)/potassium phosphates liquid biphasic system (LBS) to extract gamma-cyclodextrin (γ-CD) was examined. A range of EOPO (with potassium phosphates) molecular weights was screen to investigate the effect of the latter on the partioning efficency of CGTase and γ-CD. The results show that the optimal top phase γ-CD yield (74.4%) was reached in 35.0% (w/w) EOPO 970 and 10.0% (w/w) potassium phosphate with 2.0% (w/w) sodium chloride. A theoretical explanation for the effect of NaCl on γ-CD was also presented. After a 2 h bioconversion process, a total of 0.87 mg/mL concentration of γ-CD was produced in the EOPO/ phosphates LBS top phase. After the extraction of top phase from LBS, four continuous repetitive batches were successfully conducted with relative CGTase activity of 1.00, 0.86, 0.45, and 0.40 respectively.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Extractive Bioconversion of Gamma-Cyclodextrin and Recycling of Cyclodextrin Glycosyltransferase in Liquid Biphasic System Using Thermo-Separating Polymer

et al. 2018

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“…With mass spectrometry, we then identified a cyclomaltodextrin glucanotransferase (CGTase) from Thermoanaerobacterium thermosulfurigenes in the aroma ( Figure 5 , Table S3 ). CGTases are used in the starch industry to modify starch [ 30 , 31 , 32 , 33 , 34 ]. They convert starch into linear and cyclic oligosaccharides, so-called ring-shaped dextrins (cyclodextrins) [ 30 , 31 , 32 , 33 ].…”

Section: Discussionmentioning

confidence: 99%

“…CGTases are used in the starch industry to modify starch [ 30 , 31 , 32 , 33 , 34 ]. They convert starch into linear and cyclic oligosaccharides, so-called ring-shaped dextrins (cyclodextrins) [ 30 , 31 , 32 , 33 ]. These cyclodextrins are used in food additives as carriers of aromas, to stabilize fat-soluble colorants and to improve aroma (e.g., to reduce the undesirable aftertaste in sweeteners) [ 12 , 35 ].…”

Section: Discussionmentioning

confidence: 99%

Pudding Proteomics: Cyclomaltodextrin Glucanotransferase and Microbial Proteases Can Liquefy Extended Shelf Life Dairy Products

Kleinwort¹,

Weigand²,

Hoffmann³

et al. 2022

Metabolites

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In recent years, a lack of stability of dairy products with extended shelf life (e.g., yoghurt products, UHT desserts) has occurred, with the corresponding products liquefying significantly after days or weeks. This project aimed to identify the enzymes responsible for the liquefaction of the affected products based on differential proteomic analyses. No evidence was found for the presence of starch-degrading bacteria in the affected products. With zymography and proteome analysis, we detected the cause of liquefaction in a pudding by contamination of its aroma component with an engineered amylolytic enzyme, cyclomaltodextrin glucanotransferase (CGTase) from Thermoanaerobacterium thermosulfurigenes. In addition, we detected contamination with Pseudomonas-derived proteolytic ATP-dependent Clp protease in one pudding batch and proteases in technically used amylases, which degraded β-caseins in another batch. Identification of these agents with liquefying properties in dairy products are useful for adjustment of production protocols and/or composition of additives, and thus shelf life extension.

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“…The extraction of products into the solvent-rich phase due to its affinity to the solvent infiltrates the microbial cells and substrates into the raffinate phase, making it a superior technique compared to conventional separation methods (12)(13)(14)(15). Earlier investigation reported the usage of neoteric solvents such as ionic liquids and deep eutectics as the most effective phase-forming components in the purification of therapeutic enzymes (16)(17)(18)(19). However, the hydrophilicity of these solvents alleviates the demand for higher concentrations, posing potential challenges in making the process viable on a large scale (20).…”

Section: Introductionmentioning

confidence: 99%

Switchable deep eutectic solvent driven micellar extractive fermentation of ultrapure fibrin digesting enzyme from Bacillus subtilis

Muniasamy

Rathnasamy

2021

Preprint

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Fibrinolytic protease (FLP) is a therapeutic enzyme used in the treatment of thrombolytic diseases. The present study proposed the concept of pH-driven swappable micellar two-phase extraction for the concurrent production and purification of FLP from Bacillus subtilis at cloud point extraction. Extractive fermentation was carried out with a pH swap mechanism, and FLP was extracted to the top phase by surfactant deep eutectic solvents (SADES). Shrimp waste was chosen as a sustainable low-cost substrate that yielded a maximum protease of 185 U/mg. Six SDESs were synthesized with nonionic surfactants as hydrogen bond donors and quaternary ammonium salts as hydrogen bond acceptors, and their association was confirmed by H1 NMR. Thermophysical investigation of the synthetic SADES was accomplished as a function of temperature. Response surface methodology for extractive fermentation was performed with the concentration of SADES (35% w/v), Na2SO4 (15% w/v) and pH (6.3) as variables and the enzyme activity (248 IU/mg) as a response. Furthermore, purification using gel filtration chromatography was used to quantify the amount of enzyme obtained in the extraction phase (849 IU/ml). After final purification with an anion exchange column, the maximum purity fold (22.32) with enzyme activity (1172 IU/ml) was achieved. The in vitro fibrinolytic activity was confirmed using a fibrin plate assay.

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Production of γ-cyclodextrin by Bacillus cereus cyclodextrin glycosyltransferase using extractive bioconversion in polymer-salt aqueous two-phase system

Cited by 18 publications

References 20 publications

Extractive Bioconversion of Gamma-Cyclodextrin and Recycling of Cyclodextrin Glycosyltransferase in Liquid Biphasic System Using Thermo-Separating Polymer

Extractive Bioconversion of Gamma-Cyclodextrin and Recycling of Cyclodextrin Glycosyltransferase in Liquid Biphasic System Using Thermo-Separating Polymer

Pudding Proteomics: Cyclomaltodextrin Glucanotransferase and Microbial Proteases Can Liquefy Extended Shelf Life Dairy Products

Switchable deep eutectic solvent driven micellar extractive fermentation of ultrapure fibrin digesting enzyme from Bacillus subtilis

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