Mutations at calcium binding site III in cyclodextrin glycosyltransferase improve β-cyclodextrin specificity

Ban, Xiaofeng; Gu, Zhennan; Li, Caiming; Huang, Min; Cheng, Li; Yan, Hong; Li, Zhaofeng

doi:10.1016/j.ijbiomac.2015.02.036

Cited by 10 publications

(3 citation statements)

References 32 publications

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“…Specific changes in residues involved in the catalytic site of the enzyme can affect enzymesubstrate interactions, thus driving the type of product obtained. This has been demonstrated for positions (as referred to Bacillus circulans 251 CGTase) 77 and 239 (Kelly et al, 2008), 43, 137-144 and 188 (Goh et al, 2009), 47 (Li et al, 2009a), 93 (Rostinawati et al, 2015), 89 and 372 (Li et al, 2009b), 179 (Costa et al, 2012), 195 (Xie et al, 2014a2014b), 315 (Ban et al, 2015), 577 (Huang et al, 2014;Li et al, 2016) and 100, 227 and 328 (Wang et al, 2017). Nevertheless, the mechanism determining the size of the synthesized CD remains unknown.…”

Section: Introductionmentioning

confidence: 96%

“…As mentioned above, all CGTases isolated so far produce a mixture of CD when they are incubated with starch, and CD purification from the reaction mixture is the main difficulty encountered during CD production. Recently, different researchers have attempted to direct the synthesis towards a single type of cyclodextrin (Li et al, 2007;Wu et al, 2012;Wang et al, 2013) or to obtain enzymes with improved product yield and specificity (Li et al, 2007;Wang et al, 2013;Han et al, 2014;Huang et al, 2014;Xie et al, 2014a;Ban et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

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A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Castillo

Landriel

Sánchez-Costa

et al. 2018

Protein Engineering, Design and Selection

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Cyclodextrin glycosyltransferases (CGTases) are bacterial enzymes that catalyze starch conversion into cyclodextrins, which have several biotechnological applications including solubilization of hydrophobic compounds, masking of unpleasant odors and flavors in pharmaceutical preparations, and removal of cholesterol from food. Additionally, CGTases produce maltooligosaccharides, which are linear molecules with potential benefits for human health. Current research efforts are concentrated in the development of engineered enzymes with improved yield and/or particular product specificity. In this work, we analyzed the role of four residues of the CGTase from Paenibacillus barengoltzii as determinants of product specificity. Single mutations were introduced in the CGTase-encoding gene to obtain mutants A137V, A144V, L280A and M329I and the activity of recombinant proteins was evaluated. The residue at position 137 proved to be relevant for CGTase activity. Molecular dynamics studies demonstrated additionally that mutation A137V produces a perturbation in the catalytic site of the CGTase, which correlates with a 10-fold reduction in its catalytic efficiency. Moreover, this mutant showed increased production of maltooligosaccharides with a high degree of polymerization, mostly maltopentaose to maltoheptaose. Our results highlight the role of residue 137 as a determinant of product specificity in this CGTase and may be applied to the rational design of saccharide-producing enzymes.

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Section: Introductionmentioning

confidence: 96%

Section: Introductionmentioning

confidence: 99%

A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Castillo

Landriel

Sánchez-Costa

et al. 2018

Protein Engineering, Design and Selection

View full text Add to dashboard Cite

show abstract

“…In an aqueous solution, due to hydrogen bonding between β-CD molecules and water molecules, β-CD molecules trap the poor water-soluble guest molecule in the cavity in β-CD, forming a stable host-guest molecule [20]. The hydrophobic groups of the SH molecule can interact with the hydrophobic groups inside the cavity in β-CD to generate a complex and improve its solubility, stability, antioxidant activity, and bioavailability [21,22].…”

Section: Introductionmentioning

confidence: 99%

Study on the Antioxidant Effect of Shikonin-Loaded β-Cyclodextrin Forming Host–Guest Complexes That Prevent Skin from Photoaging

Yue,

Fang,

Jia

et al. 2023

IJMS

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When the skin is overexposed to ultraviolet rays, free radicals will accumulate in the skin, causing lipid damage and even inducing photoaging of the skin. Combination therapy with antioxidant drugs is a good choice for topical treatment of skin photoaging due to its special physiological structure. In this paper, shikonin was encapsulated in β-cyclodextrin (SH-β-CD) by the precipitation crystallization method, which delayed the release of the drug and increased drug solubility. The average diameter of SH-β-CD was 203.0 ± 21.27 nm with a zeta potential of −14.4 ± 0.5 mV. The encapsulation efficiency (EE%) was 65.9 ± 7.13%. The results of the in vitro permeation across the dialysis membrane and ex vivo transdermal release rates were 52.98 ± 1.21% and 88.25 ± 3.26%, respectively. In vitro antioxidant and antilipid peroxidation model assay revealed the antioxidant potential of SH and SH-β-CD. In the mice model of skin photoaging, SH and SH-β-CD had a recovery effect on the skin damage of mice, which could significantly increase the superoxide dismutase (SOD) activity in the skin. Briefly, SH-β-CD had an obvious therapeutic effect on the skin photoaging of mice caused by UV, and it is promising in skin disease treatment and skin care.

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Mathematical modelling and kinetic study for CD production catalysed by Toruzyme® and CGTase from Bacillus firmus strain 37

Pinheiro

Nascimento

Fenelon

et al. 2017

Bioprocess Biosyst Eng

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A new mathematical model was developed for the kinetics of α-, β- and γ-cyclodextrin production, expanding an existing model that only included the production of β- and γ-cyclodextrins, because a detailed kinetic modelling of the reactions involved allows the manipulation of the process yields. The kinetic behaviour of the commercial enzyme Toruzyme was studied with maltodextrin as substrate at different concentrations and for CGTase from Bacillus firmus strain 37 at a concentration of 100 g L. The mathematical model showed a proper fit to the experimental data, within the 24-h period studied, confirming that the considered hypotheses represent the kinetic behaviour of the enzymes in the reaction medium. The kinetic parameters generated by the model allowed reproducing previous observed qualitative tendencies as it can be seen that changing experimental conditions in the reaction process such as enzyme and substrate concentrations results in large changes in the enzyme kinetics and using high substrate concentrations does not guarantee the highest conversion rates due to enzyme inhibition and reverse reactions. In addition, this new mathematical model complements previous qualitative observations enabling the manipulation of the direct and reverse reactions catalysed by the enzyme by adjusting the reaction conditions, to target quantitative results of increased productivity and better efficiency in the production of a desired cyclodextrin.

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Mutations at calcium binding site III in cyclodextrin glycosyltransferase improve β-cyclodextrin specificity

Cited by 10 publications

References 32 publications

A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

A single mutation in cyclodextrin glycosyltransferase from Paenibacillus barengoltzii changes cyclodextrin and maltooligosaccharides production

Study on the Antioxidant Effect of Shikonin-Loaded β-Cyclodextrin Forming Host–Guest Complexes That Prevent Skin from Photoaging

Mathematical modelling and kinetic study for CD production catalysed by Toruzyme® and CGTase from Bacillus firmus strain 37

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