Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant

Escobar, Sindy; Bernal, Claudia; Mesa, Mónica

doi:10.1016/j.bej.2013.03.010

Cited by 14 publications

(17 citation statements)

References 43 publications

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“…Taking into account that the enzyme deactivation during this stage is less than 5% and there is no difference between SolT0 and SolT3 with α = 0.05 (Figure 4(b)), it can be concluded that the surfactant effect on the enzyme is more important during the first step of the encapsulation process, as it was shown for the free enzyme and in the silica sol ( Figure 1). In spite of this initial loss of activity, Journal of Biomaterials Science, Polymer Edition 7 the enzyme stability in these β-gal/silica derivatives is higher when these biocatalysts are prepared in the presence of Triton X-100 surfactant (Figure 4(c)) in a similar way that it was seen for the soluble enzyme, [20] demonstrating the protective role of this non-ionic surfactants on the encapsulated enzymes.…”

Section: Effect Of the Surfactantmentioning

confidence: 61%

“…[25] These initial conformational changes in the presence of 1 × 10 −3 M Triton X-100 is the cost that the enzyme must pay for gaining a more stable conformation to long-term, [20] as it was shown in its kinetic study in the presence of Triton X-100 and that will affect the performance of the final β-gal/silica biocatalysts.…”

Section: Effect Of the Silica Sol Conditions On The Soluble β-Gal Behmentioning

confidence: 97%

“…This is a monomeric globular isoform, exhibiting 212-240 kDa molecular weight; its maximal activity is expressed at pH 6.0 and 45°C. According to the kinetic study, [20] this enzymatic extract exhibits longer lifetime at pH 6.0 in the presence of 1 × 10 −3 M Triton X-100. These conditions are taken into account in this work for designing the encapsulation route of β-gal B. circulans in silica by sol-gel process assisted by Triton X-100 surfactant.…”

Section: Introductionmentioning

confidence: 99%

“…[2,18,19] The interaction of β-gal with Triton X-100, which is a non-ionic, ecofriendly, inexpensive, nontoxic surfactant, has been less studied, but its effect is less deleterious over the β-gal due to the absence of charge, and it helps to stabilize this enzyme in aqueous solution. [20] The β-gal from Bacillus circulans (β-gal B. circulans) is present as three isoforms in crude extracts. [16] The isoenzyme I predominates in the commercial extract used in this work.…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Relationship between sol–gel conditions and enzyme stability: a case study with β-galactosidase/silica biocatalyst for whey hydrolysis

Escobar

Bernal

Mesa

2015

Journal of Biomaterials Science, Polymer Edition

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The sol-gel process has been very useful for preparing active and stable biocatalysts, with the possibility of being reused. Especially those based on silica are well known. However, the study of the enzyme behavior during this process is not well understood until now and more, if the surfactant is involved in the synthesis mixture. This work is devoted to the encapsulation of β-galactosidase from Bacillus circulans in silica by sol-gel process, assisted by non-ionic Triton X-100 surfactant. The correlation between enzyme activity results for the β-galactosidase in three different environments (soluble in buffered aqueous reference solution, in the silica sol, and entrapment on the silica matrix) explains the enzyme behavior under stress conditions offered by the silica sol composition and gelation conditions. A stable β-galactosidase/silica biocatalyst is obtained using sodium silicate, which is a cheap source of silica, in the presence of non-ionic Triton X-100, which avoids the enzyme deactivation, even at 40 °C. The obtained biocatalyst is used in the whey hydrolysis for obtaining high value products from this waste. The preservation of the enzyme stability, which is one of the most important challenges on the enzyme immobilization through the silica sol-gel, is achieved in this study.

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Section: Effect Of the Surfactantmentioning

confidence: 61%

Section: Effect Of the Silica Sol Conditions On The Soluble β-Gal Behmentioning

confidence: 97%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Relationship between sol–gel conditions and enzyme stability: a case study with β-galactosidase/silica biocatalyst for whey hydrolysis

Escobar

Bernal

Mesa

2015

Journal of Biomaterials Science, Polymer Edition

Self Cite

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“…In contrast, electrochemical methods are simple, inexpensive, and reliable approaches for the detection of nicotine [6][7][8][9]. However, they have some limitations, such as slow oxidation/reduction and low sensitivity [10][11][12]. There are two ways to improve the sensitivity of the sensing electrode, namely changing the base electrode material [8,13,14] or using the surface modifiers [15,16].…”

Section: Introductionmentioning

confidence: 92%

Evaluation of nicotine sensor based on copper nanoparticles and carbon nanotubes

et al. 2015

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An electrochemical sensor was prepared to detect nicotine by depositing copper nanoparticles (Cu NPs) on the surface of a glassy carbon electrode (GCE) modified with multi-walled carbon nanotubes (MWNTs). The modified electrode was characterized by scanning electron microscopy and cyclic voltammetry. The novel-modified sensor exhibited effective electrocatalytic activities toward anodic oxidation of nicotine. Calibration plot showed two linear regions with different sensitivity, 1.121 (r 2 = 0.982) in the range from 1 9 10 -6 to 9 9 10 -5 M and 0.164 (r 2 = 0.982) from 1 9 10 -4 M up to 1 9 10 -3 M. The detection limit was 1 lM. For six parallel detections of 1 mM nicotine, the relative standard deviation was 5.68 %, suggesting that the film-modified electrode had good reproducibility. Experimental parameters affecting the sensor response such as pH, modifier concentration and electrodeposition scan rate were found to be optimum at 7.0, 2 mg mL -1 and 80 mV s -1 , respectively.

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Thermostabilization of Aspergillus oryzae β‐d‐galactosidase

Wahba

2015

Biotech and App Biochem

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The thermal stability of the Aspergillus oryzae β-d-galactosidase (β-gal) was evaluated at 60 °C. The stability of β-gal was dependent on the pH, buffer, and additives. The β-gal exhibited its highest thermal stability in a 0.02 M phosphate buffer pH 6. Among all the tested additives, galactose, a competitive inhibitor of β-gal, was the upmost thermal stabilizer. A 0.15 M galactose solution caused β-gal to retain a whole of 98.65% of its initial activity after incubation at 60 °C for 2 H. The second best thermal stabilizer of β-gal was raffinose. A 0.15 M raffinose-β-gal mixture retained 84.41% of its initial activity after incubation at 60 °C for 2 H, whereas the control retained only 61.02%. The results of this study also revealed that all the tested positively charged polymers (diethylaminoethyl [DEAE] dextran and polyethyleneimine [PEI] 800, 2,000, 750,000 Da) significantly destabilized β-gal. However, these positively charged polymers exerted different effects on the β-gal's activity. PEI 750,000 significantly activated the enzyme, while DEAE dextran and PEI 800 did not exert any significant effects on the β-gal's activity. Nevertheless, PEI 2,000 significantly activated the enzyme.

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Kinetic study of the colloidal and enzymatic stability of β-galactosidase, for designing its encapsulation route through sol–gel route assisted by Triton X-100 surfactant

Cited by 14 publications

References 43 publications

Relationship between sol–gel conditions and enzyme stability: a case study with β-galactosidase/silica biocatalyst for whey hydrolysis

Relationship between sol–gel conditions and enzyme stability: a case study with β-galactosidase/silica biocatalyst for whey hydrolysis

Evaluation of nicotine sensor based on copper nanoparticles and carbon nanotubes

Thermostabilization of Aspergillus oryzae β‐d‐galactosidase

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