Kinetics of thermal inactivation of free Aureobasidium pullulans fructosyltransferase

Onderková, Z.; Bryjak, Jolanta; Vaňková, Katarína; Polakovič, Milan

doi:10.1016/j.enzmictec.2010.06.009

Cited by 17 publications

(5 citation statements)

References 19 publications

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“…During industrial application, enzymes are subject to denaturation upon variation of temperature and prolonged exposure. Therefore, a long‐term operational stability of an enzyme preparation is a common prerequisite of successful operation of an enzyme‐based bioprocess . Then, to evaluate FFase thermostability, long‐term residual activity tests were carried out in the temperature range of 45–65°C, whose results in terms of residual activity coefficient ( ψ ) are illustrated in Figure .…”

Section: Resultsmentioning

confidence: 99%

“…Therefore, a long-term operational stability of an enzyme preparation is a common prerequisite of successful operation of an enzyme-based bioprocess. 41 Then, to evaluate FFase thermostability, long-term residual activity tests were carried out in the temperature range of 45-65 C, whose results in terms of residual activity coefficient (ψ) are illustrated in Table 4 together with those of other kinetic and thermodynamic parameters of enzyme thermal inactivation. In the above tested temperature range, FFase showed the typical decay of classic first-order denaturation pattern observed by Onderková et al 41 for FTase from Aureobasidium pullulans.…”

Section: Kinetic and Thermodynamic Parameters Of Ffase Thermal Inacmentioning

confidence: 99%

“…41 Then, to evaluate FFase thermostability, long-term residual activity tests were carried out in the temperature range of 45-65 C, whose results in terms of residual activity coefficient (ψ) are illustrated in Table 4 together with those of other kinetic and thermodynamic parameters of enzyme thermal inactivation. In the above tested temperature range, FFase showed the typical decay of classic first-order denaturation pattern observed by Onderková et al 41 for FTase from Aureobasidium pullulans. One can see that k d progressively increased with temperature, which means that the inactivation became progressively more significant, likely due to breaking of strong electrostatic bonds.…”

Section: Kinetic and Thermodynamic Parameters Of Ffase Thermal Inacmentioning

confidence: 99%

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Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Oliveira

Silva

Converti

et al. 2019

Biotechnology Progress

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This study reports on the biochemical characterization as well as the kinetic and thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase (FFase) with transfructosylating activity. Conditions for FFase activity were optimized by means of a central composite rotational design using pH and temperature as the independent variables, while residual activity tests carried out in the temperature range of 45–65°C enabled us to investigate FFase thermostability and estimate the kinetic and thermodynamic parameters of enzyme denaturation. Optimal conditions for sucrose hydrolysis and fructosyl transfer catalyzed by crude FFase were 50°C, and pH 6.0 and 7.4, respectively. The thermodynamic properties of irreversible enzyme inactivation were found to be activation energy of 293.1 kJ mol−1, and activation enthalpy, entropy, and Gibbs free energy in the ranges 290.3–290.4 kJ mol−1, 568.7–571.0 J mol−1 K−1, and 97.9–108.8 kJ mol−1, respectively. The results obtained in this study point out satisfactory enzyme activity and thermostability at temperatures commonly used for industrial fructo‐oligosaccharide (FOS) synthesis; therefore, this novel FFase appears to be a promising biocatalyst with great potential for long‐term FOS synthesis and invert sugar production. To the best of our knowledge, this is the first report on kinetic and thermodynamic parameters of an A. tamarii FFase.

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Section: Resultsmentioning

confidence: 99%

Section: Kinetic and Thermodynamic Parameters Of Ffase Thermal Inacmentioning

confidence: 99%

Section: Kinetic and Thermodynamic Parameters Of Ffase Thermal Inacmentioning

confidence: 99%

See 1 more Smart Citation

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Oliveira

Silva

Converti

et al. 2019

Biotechnology Progress

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show abstract

“…This is due to an enzyme's ability to maintain its activity under elevated temperatures or other extreme circumstances, thereby expanding its potential applications in the industrial sector 28 . In this particular instance, certain researchers have additionally noted that the activity of both enzymes adheres to the customary decay pattern of the classic first‐order denaturation 29 . The primary kinetic parameters of the thermal inactivation of both enzymes were approximated based on the linear trends depicted in Fig.…”

Section: Resultsmentioning

confidence: 99%

“…28 In this particular instance, certain researchers have additionally noted that the activity of both enzymes adheres to the customary decay pattern of the classic first-order denaturation. 29 The primary kinetic parameters of the thermal inactivation of both enzymes were approximated based on the linear trends depicted in Fig. 5(b), and the correlation was deemed satisfactory (R 2 ≥ 0.96).…”

Section: Structural and Chemical Characterization Of Modified Depsmentioning

confidence: 99%

Tailored chitosan integration in diatomaceous earth particles as a scaffold for fructosyltransferase immobilization in fructo‐oligosaccharide production

Zhao,

Xiao,

Jiang

et al. 2024

J Sci Food Agric

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BackgroundFructo‐oligosaccharide (FOS) belongs to the group of short inulin‐type fructans and is one of the most important non‐digestible bifido‐oligosaccharides capable of biotransforming sucrose using fructosyltransferases (FTase). However, there are no immobilized FTase products that can be successfully used industrially. In this study, diatomite was subjected to extrusion, sintering, and granulation to form diatomaceous earth particles that were further modified via chitosan aminomethylation for modification. FTase derived from Aspergillus oryzae was successfully immobilized on the modified support via covalent binding.ResultsThe immobilized enzyme activity was 503 IU g−1 at an enzyme concentration of 0.6 mg mL−1, immobilization pH of 7.0, and contact time of 3 h. Additionally, the immobilization yield was 56.91%. Notably, the immobilized enzyme is more stable under acidic conditions. Moreover, half‐life of the immobilized enzyme was 20.80 and 10.96‐times as long as the free enzyme at 45 and 60 °C, respectively. This study shows good reusability, as evidenced by the 84.77% retention of original enzyme activity after eight cycles. Additionally, the column transit time of the substrate was approximately 35.56 min when the immobilized enzyme was applied in a packed‐bed reactor. Furthermore, a consistently high FOS production yield of approximately 60.68% was achieved and maintained over the 15‐d monitoring period.ConclusionsOur results suggest that immobilized FTase as a viable candidate for continuous FOS production on an industrial scale.This article is protected by copyright. All rights reserved.

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Overproduction, purification, and property analysis of an extracellular recombinant fructosyltransferase

Guo

Yang

Qiang

et al. 2015

Eur Food Res Technol

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Kinetics of thermal inactivation of free Aureobasidium pullulans fructosyltransferase

Cited by 17 publications

References 19 publications

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Biochemical characterization and kinetic/thermodynamic study of Aspergillus tamarii URM4634 β‐fructofuranosidase with transfructosylating activity

Tailored chitosan integration in diatomaceous earth particles as a scaffold for fructosyltransferase immobilization in fructo‐oligosaccharide production

Overproduction, purification, and property analysis of an extracellular recombinant fructosyltransferase

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