Kinetic and thermodynamic features of nanomagnetic cross-linked enzyme aggregates of naringinase nanobiocatalyst in naringin hydrolysis

Torabizadeh, Homa; Mikani, Mohaddeseh

doi:10.1016/j.ijbiomac.2018.08.005

Cited by 16 publications

(5 citation statements)

References 48 publications

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“…Moreover, naringinase from Aspergillus aculeatus has been immobilized onto magnetic Fe 3 O 4 nanoparticles [34]. A method for obtaining nanomagnetic cross-linked enzyme aggregates of naringinase has also been developed [35,36]. The naringinase subunit α- l -rhamnosidase of Aspergillus terreus was covalently immobilized on three magnetic supports (Dacron-hydrazide, polysiloxane/polyvinyl alcohol (POS/PVA), and chitosan) [37].…”

Section: Introductionmentioning

confidence: 99%

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Bodakowska-Boczniewicz

Garncarek

2019

Molecules

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Naringinase is an enzyme complex which exhibits α-l-rhamnosidase and β-d-glucosidase activity. This enzymatic complex catalyzes the hydrolysis of naringin (4′,5,7-trihydroxy flavanone 7-rhamnoglucoside), the main bittering component in grapefruit. Reduction of the level of this substance during the processing of juice has been the focus of many studies. The aim of the study was the immobilization of naringinase on chitosan microspheres activated with glutaraldehyde and, finally, the use of such immobilized enzyme for debittering grapefruit juice. The effect of naringinase concentration and characterization of the immobilized enzyme compared to the soluble enzyme were investigated. The maximum activity was observed at optimum pH 4.0 for both free and immobilized naringinase. However, the optimum temperature was shifted from 70 to 40 °C upon immobilization. The KM value of the immobilized naringinase was higher than that of soluble naringinase. The immobilization did not change the thermal stability of the enzyme. The immobilized naringinase had good operational stability. This preparation retained 88.1 ± 2.8% of its initial activity after ten runs of naringin hydrolysis from fresh grapefruit juice. The results indicate that naringinase immobilized on chitosan has potential applicability for debittering and improving the sensory properties of grapefruit juices.

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Section: Introductionmentioning

confidence: 99%

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Bodakowska-Boczniewicz

Garncarek

2019

Molecules

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“…The maximum enzyme activity (V max ) and the minimum concentration of substrate (K m ) required to saturate isolated naringinase were determined by calculating the reaction rate at increasing substrate concentration 24 . Naringin was used at different concentrations for determining the optimal conditions of enzyme activity 25 .…”

Section: Methodsmentioning

confidence: 99%

Simultaneous production and sustainable eutectic mixture based purification of narringinase with Bacillus amyloliquefaciens by valorization of tofu wastewater

Balaraman

Purushotaman

Chandramouliswaran

et al. 2022

Sci Rep

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The current investigation is being executed for sustainable one-pot production and purification of naringinase using natural deep eutectic solvent-based extractive fermentation. Five natural deep eutectic solvents were prepared and their physicochemical properties were determined as a function of temperature. Tofu wastewater was used as a low-cost substrate for naringinase production and simultaneous in-situ purification of the enzyme was accomplished by employing NADES. Optimal conditions of influential factors like concentrations of NADES (74.5% w/w), Na2SO4 (15% w/v) and tofu wastewater (1.5% w/w) resulted in an effective yield of naringinase (249.6 U/ml). Scale-up of naringinase production with a 3 l custom made desktop bioreactor was accomplished and effective regeneration of NADES was established. NADES exhibits selectivity during extraction even after the fifth cycle proving it to be tailor-made. The resulting active enzyme was quantified by size exclusion chromatography (736.85 U/mg). Ultrapure enzyme fraction was obtained with anion exchange chromatography yielding maximum purity of (63.2 U/ml) and specific naringinase activity of (3516 U/mg). The in-vitro debittering activity of the resulting ultrapure enzyme fraction was determined with grape juice resulting in naringin and limonin removal of [23.4% (w/w)] and [64.3% (w/w)] respectively.

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“…The maximum rate of enzyme activity (V max ) and the minimum concentration of substrate (K m ) required to saturate the enzyme was determined by calculating the rate of reaction at increasing substrate concentration 30 . Naringin was used as substrate and was taken at different concentration for determining the optimal conditions of enzyme activity 31 .…”

Section: Enzyme Kineticsmentioning

confidence: 99%

Simultaneous Production and Sustainable Eutectic Mixture Based Purification of Narringinase With Bacillus Amyloliquefaciens by Valorization of Tofu Wastewater

Balaraman

Purushotaman

Chandramouliswaran

et al. 2022

Preprint

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Sustainable one-pot production and purification of naringinase using natural deep eutectic solvent based extractive fermentation is being executed in the current investigation. Tofu wastewater was used as alternative low-cost media for sustainable production of naringinase. Five natural deep eutectic solvents were prepared and their physicochemical properties were determined as a function of temperature. Optimization of essential variables in extractive fermentation for determining effective concentration of NADES at (74.5% w/w), Na2SO4 (15% w/v) and tofu wastewater (1.5% w/w) to achieve optimal naringinase yield of (249.6 U/ml). Scale up of naringinase production with a 3 L custom made desktop bioreactor was accomplished and effective regeneration of NADES was established. Quantification of the resulting active enzyme was done by size exclusion chromatography (736.85 U/mg). Ultrapure enzyme fraction was obtained with anion exchange chromatography yielding maximum purity of (63.2) and specific enzyme activity of (3516 U/mg). The in-vitro debittering activity of resulting ultrapure naringinase was determined with grape juice.

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Kinetic and thermodynamic features of nanomagnetic cross-linked enzyme aggregates of naringinase nanobiocatalyst in naringin hydrolysis

Cited by 16 publications

References 48 publications

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Immobilization of Naringinase from Penicillium decumbens on Chitosan Microspheres for Debittering Grapefruit Juice

Simultaneous production and sustainable eutectic mixture based purification of narringinase with Bacillus amyloliquefaciens by valorization of tofu wastewater

Simultaneous Production and Sustainable Eutectic Mixture Based Purification of Narringinase With Bacillus Amyloliquefaciens by Valorization of Tofu Wastewater

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