Kinetic and thermodynamic characteristic of Aspergillus awamori EM66 levansucrase

Mostafa, Faten A.; Wahab, Walaa A. Abdel; Salah, Hala A.; Nawwar, Galal A. M.; Esawy, Mona A.

doi:10.1016/j.ijbiomac.2018.07.111

Cited by 30 publications

(25 citation statements)

References 39 publications

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Section: Resultssupporting

confidence: 86%

“…Therefore, we can infer that both reactions catalyzed by A. tamarii FFase were kinetically controlled by temperature within the entire temperature range investigated. Similar results were reported for a partially purified (1.33) and a purified levansucrase (1.24) from A. awamori 44. Values of the activation enthalpy (ΔH * ), entropy (ΔS * ), and Gibbs free energy (ΔG * ) of the reactions catalyzed by FFase from A. tamarii are listed inTable 5.…”

supporting

confidence: 79%

“…Moreover, this value is very close to that estimated for a free fructosyltransferase from Rhodotorula sp. (294.35 kJ mol −1 ), but significantly higher than those of prepurified (136 kJ mol −1 ) and purified (98 kJ mol −1 ) levansucrase from Aspergillus awamori …”

Section: Resultsmentioning

confidence: 86%

“…(294.35 kJ mol −1 ), 43 but significantly higher than those of prepurified (136 kJ mol −1 ) and purified (98 kJ mol −1 ) levansucrase from Aspergillus awamori. 44 As is known, E * d is directly related to the activation enthalpy of thermal denaturation (ΔH * d ), which is the total amount of thermal energy required to denature the enzyme and is related to the number of noncovalent bonds broken during the denaturation process. [45][46][47] The positive and large values of ΔH * d estimated for A. tamarii FFase (290.4-290.3 kJ mol −1 ) ( Table 4) are consistent with the fact that enzyme denaturation is an endothermic process and with its high thermostability.…”

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: Resultssupporting

confidence: 86%

supporting

confidence: 79%

Section: Resultsmentioning

confidence: 86%

Section: Kinetic and Thermodynamic Parameters Of Ffase Thermal Inacmentioning

confidence: 99%

See 2 more Smart Citations

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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“…The study by Ferreira et al [36], indicated that lipase from Geotrichum candidum required 34.50 kJ/mol of activation energy. While lipase from Aspergillus awamori as studied by Mostafa et al [37], required 32.75 kJ/mol activation energy, and 10.54 kJ/mol activation energy was needed by lipase from Candida rugosa as claimed by Onoja et al [38]. From the data, the activation energy was different according to the other kind of lipase.…”

Section: Effect Of Lipase Activity Towards Temperaturementioning

confidence: 88%

Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil

Gusniah

Veny

Hamzah

2020

Bull. Chem. React. Eng. Catal.

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Biodiesel is fatty acid methyl ester that commonly derived from vegetable oils and animal fats that can be produced through enzymatic transesterification using lipase. In this study, three different types of lipase were used, which are Lipase Immobilized Pseudomonas cepacia, PcL, Thermomyces lanuginosus, TLIM, and Candida Antarctica A (recombinant from Aspergillus oryzae), CALA. These lipases were compared based on their activity at different pH (6-10), temperature (30-50 °C), activation energy, and amount of lipase loading for hydrolysis of p-NPA into n-NP. The result indicates that among the lipase used in the study, CALA is the preferable biocatalyst in the hydrolysis of p-NPA due to the minimum energy required and higher enzymatic activity at 20 mg of enzyme loading. PcL and CALA used in the study gave the optimum activity at pH 9 except for TLIM at pH 8 and the optimum temperature at 40 °C. The kinetic data obtained for CALA in this reaction were Km = 57.412 mM and Vm = 70 µM/min. This finding shows that CALA is beneficial biocatalysts for the transesterification process to obtain a higher product with lower activation energy. Copyright © 2020 BCREC Group. All rights reserved

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Characterization of a new efficient low molecular weight Bacillus subtilis NRC₁₆ levansucrase and its levan

et al. 2019

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Screening of 18 bacterial honey isolates revealed that all the isolates were levansucrase producers. The most potent isolate that achieved the highest activity (45.66 U/ml) was identified as Bacillus subtilis NRC based on morphological examination and 16S rRNA. The results recorded the necessity of starch (5 g/L), baker's yeast (12.5 g/L), and AlCl 3 (5 mM) in improvement of the enzyme productivity. The Bacillus subtilis levansucrase was eluted as a single protein in one purification step. The enzyme molecular weight was (14 kDa). It showed its optimum activity at 45°C and could retain 60% of its activity after incubation at 50°C for 2 h. Its optimum activity was obtained at pH 8.2 and the enzyme showed great pH stability in both acidic and alkaline ranges.Unlike, most levansucrases all tested metals had an adverse effect in enzyme activity. The enzyme had antioxidant activities and were characterized as spherical micro-and nanoparticles by transmission electron microscopy. The effect of growth conditions and medium composition in levan structure and its fibrinolytic activity was evaluated. K E Y W O R D S

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Kinetic and thermodynamic characteristic of Aspergillus awamori EM66 levansucrase

Cited by 30 publications

References 39 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

Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil

Characterization of a new efficient low molecular weight Bacillus subtilis NRC₁₆ levansucrase and its levan

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Kinetic and thermodynamic characteristic of Aspergillus awamori EM66 levansucrase

Cited by 30 publications

References 39 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

Activity and Stability of Immobilized Lipase for Utilization in Transesterification of Waste Cooking Oil

Characterization of a new efficient low molecular weight Bacillus subtilis NRC16 levansucrase and its levan

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Characterization of a new efficient low molecular weight Bacillus subtilis NRC₁₆ levansucrase and its levan