Biochemical characterization of extracellular fructosyltransferase from Aspergillus oryzae IPT-301 immobilized on silica gel for the production of fructooligosaccharides

Faria, Larissa Lemos; Morales, Sergio Andrés Villalba; Prado, José Pedro Zanetti; Dias, Giancarlo de Souza; Almeida, Alex Fernando de; Xavier, Michelle da Cunha Abreu; Silva, Elda Sabino da; Maiorano, Alfredo Eduardo

doi:10.1007/s10529-020-03016-7

Cited by 17 publications

(82 citation statements)

References 59 publications

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“…The initial pH of the culture medium was adjusted to 5.5 before sterilization. The flasks were inoculated with 0.5 mL of a previously prepared suspension of 10 7 spores mL -1 , and incubated in orbital shaker at 30 ºC, 200 rpm for 64 h (Cunha et al, 2019;Faria et al, 2021). At the end of fermentation, the culture broth was vacuum-filtered (Whatman nº1) and the resulting supernatant containing an activity of 12.34 ± 0.23 U mL -1 for the FTase from A. oryzae IPT-301 was employed for further studies.…”

Section: Microorganism and Production Of The Extracellular Enzymementioning

confidence: 99%

“…The enzyme FTase (culture broth) was incubated in tris-acetate buffer at 0.2 mol L -1 and pH 5.5, in the absence of substrate, in a broad temperature range (30 ºC, 40 ºC, 50 ºC and 60 ºC). The samples were collected at specified time intervals (1 h, 2 h, 4 h and 8 h) and immediately cooled in ice bath for 5 min, and the residual activity was determined under standard conditions, according to Ottoni et al (2012), Cunha et al (2019) and Faria et al (2021). The experiments were performed in triplicate.…”

Section: Thermal Stability Assaysmentioning

confidence: 99%

“…On the other hand, the variations of the enthalpy of activation of denaturation (∆HD), Gibbs energy of activation of denaturation (∆GD) and entropy of activation of denaturation (∆SD) were calculated using Equations 4, 5 and 6, respectively (Faria et al, 2021;Gonçalves et al, 2020;Saqib et al, 2010;Souza et al, 2015).…”

Section: Thermal Stability Assaysmentioning

confidence: 99%

“…The enzyme fructosyltransferase (FTase E.C.2.4.1.9) catalyzes the reaction of sucrose transfructosylation for the production of fructooligosaccharides (FOS), fructose oligomers with degree of polymerization between two and 20, whose fructosyl units are linked to the terminal sucrose molecule by glycosidic bonds at the β-(2→1) position (Faria et al, 2021;Yun, 1996). The FOS are functional sugars with major importance for the production of foods and pharmaceuticals, since they offer several benefits to human health.…”

Section: Introductionmentioning

confidence: 99%

“…Several studies have reported optimal parameters for the production of FTase from A. oryzae IPT-301 and the behavior of its enzymatic activity according to pH, temperature and sucrose concentration (Cunha et al, 2019, Ottoni et al, 2012Perna et al, 2018). Furthermore, Faria et al (2021) and Gonçalves et al (2020) reported the enzymatic activity and thermal and operational stability of A. oryzae IPT-301 FTases immobilized by adsorption and encapsulation, respectively. Similarly, several authors have reported optimal pH and temperature values to maximize the enzymatic activity of extracellular FTases from Rhodotorula sp.…”

Section: Introductionmentioning

confidence: 99%

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Effect of temperature, pH and storage time on the stability of an extracellular fructosyltransferase from Aspergillus oryzae IPT-301

Silva

Abdal

Prado

et al. 2021

Braz. J. Food Technol.

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In this work, it was determined the influence of temperature, pH and storage time on the enzymatic activity and stability of an extracellular fructosyltransferase (FTase E.C.2.4.1.9) from Aspergillus oryzae IPT-301 produced by submerged fermentation. The thermodynamic parameters showed a tendency for increasing enzyme denaturation with the rise in temperature. The maximum transfructosylation activity was obtained at the incubation pH 5.5. During storage at 4 °C, the transfructosylation activity decreased, whereas the hydrolytic activity increased, especially in the first nine hours, a time in which the enzyme presented 45.6% of its initial transfructosylation activity. These results contributed to the improvement of the conditions of storage, immobilization and use of the soluble fructosyltransferases (FTase) in fructooligosaccharide (FOS) production.

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Section: Microorganism and Production Of The Extracellular Enzymementioning

confidence: 99%

Section: Thermal Stability Assaysmentioning

confidence: 99%

Section: Thermal Stability Assaysmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Effect of temperature, pH and storage time on the stability of an extracellular fructosyltransferase from Aspergillus oryzae IPT-301

Silva

Abdal

Prado

et al. 2021

Braz. J. Food Technol.

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Fabrication of a Simple and Cheap Screen‐printed Silver/Silver Chloride (Ag/AgCl) Quasi‐reference Electrode

Oliveira¹,

Resende

Ferreira

et al. 2021

Electroanalysis

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In this work, a silver/silver chloride ink is fabricated using two steps. First the silver ink is prepare using silver, nail polish and acetone. Then the silver ink is painted in a paper substrate and a silver chloride layer is deposited using a bleach solution. The result is the silver/ silver chloride conductive ink. The silver ink is cheap ($2.49/g), well-dispersive and very easy to fabricate. The materials were characterized by SEM and XRD. The Ag ink showed the formation of a continuous network throughout the silver ink film with fewer agglomeration.The effective chlorination process was also observed in the Ag/AgCl characterization. Since the Ag/AgCl substrate will be used as a quasi-reference electrode, it is important to investigate the electrical properties. The Ag ink showed an average ohmic resistance of 2.27 Ω. The addition of the AgCl layer decreases the conductivity, as expected. In summary, the Ag/Ag/Cl ink developed is simple, well-dispersed, cheap and with good conductivity. Therefore, it can be used as a conductive ink in the fabrication of quasi-reference electrodes.

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Study on the transfructosylation activity of Aspergillus oryzaeIPT‐301 cells in a packed bed reactor aiming at fructooligosaccharide production

Dias

Santos

Xavier

et al. 2022

J of Chemical Tech & Biotech

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BACKGROUND Fructooligosaccharides (FOS) are prebiotic sugars used in the production of functional foods. These sugars can be produced by the transfructosylation reaction of sucrose catalyzed by fructosyltransferase enzymes (FTase, E.C.2.4.1.9). The aim of this work was to evaluate the use of cells of Aspergillus oryzae IPT‐301 as biocatalysts for the sucrose transfructosylation reaction in a packed bed reactor (PBR). RESULTS The morphology of the cells was observed by scanning electron microscopy, and BET specific surface areas were examined by nitrogen physisorption The highest transfructosylation activity (660 U g−1) of the cells was obtained at 25 min of reaction by adopting a reaction temperature of 50 °C, sucrose concentration of 470 g L−1, and volumetric flow of 15 mL min−1. The rise in volumetric flow provided an increase in the transfructosylation activity, but also a faster deactivation of the biocatalyst. Enzyme kinetics was described using the Michaelis–Menten model, with a Vmax of 632.8 U g−1 and a km of 160.7 g L−1. The cells showed constant enzymatic activity for 12 h of reaction in the PBR operated with discontinuous flow at flow rates of 5 mL min−1 and 11.5 mL min−1, and in the PBR operated with continuous flow at a flow rate of 5 mL min−1. The transition from diffusional to kinetic regimes was observed starting from 11.5 mL min−1. CONCLUSION The results obtained suggest a high potential of application of the whole A. oryzae IPT‐301 cells for continuous FOS production in PBR. © 2022 Society of Chemical Industry (SCI).

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Biochemical characterization of extracellular fructosyltransferase from Aspergillus oryzae IPT-301 immobilized on silica gel for the production of fructooligosaccharides

Cited by 17 publications

References 59 publications

Effect of temperature, pH and storage time on the stability of an extracellular fructosyltransferase from Aspergillus oryzae IPT-301

Effect of temperature, pH and storage time on the stability of an extracellular fructosyltransferase from Aspergillus oryzae IPT-301

Fabrication of a Simple and Cheap Screen‐printed Silver/Silver Chloride (Ag/AgCl) Quasi‐reference Electrode

Study on the transfructosylation activity of Aspergillus oryzaeIPT‐301 cells in a packed bed reactor aiming at fructooligosaccharide production

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