Nano-magnetic cross-linked enzyme aggregates of naringinase an efficient nanobiocatalyst for naringin hydrolysis

Torabizadeh, Homa; Mikani, Mohaddeseh

doi:10.1016/j.ijbiomac.2018.05.162

Cited by 22 publications

(8 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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“…In the temperature range studied, i.e., from 25 to 55 °C, the time after which the naringinase activity is reduced to 50% of its initial activity was higher for the immobilized enzyme crosslinked with dextran aldehyde than for the free one. The half-life of naringinase from A. aculeatus immobilized in the form of aggregates with amine groups of lysine bound to Fe 3 O 4 was about 7 h at 50 °C [ 39 ].…”

Section: Resultsmentioning

confidence: 99%

“…After eight cycles of naringin hydrolysis, at 45 °C, the immobilized enzyme retained slightly over 61% of its initial activity [ 48 ]. In another study, magnetic aggregates of naringinase from A. aculeatus retained 73% of their initial activity after 10 cycles [ 39 ]. Naringinase immobilized in polyvinyl alcohol gel retained over 70% of its initial activity after eight reaction cycles at 30 °C [ 78 ].…”

Section: Resultsmentioning

confidence: 99%

“…There are only a few articles on the immobilization of naringinase on magnetic carriers in the literature [ 16 , 37 , 38 , 39 ], including one on a magnetic polysaccharide carrier [ 21 ]. However, most of these studies lack information on the thermodynamic characteristics of the immobilized enzyme.…”

Section: Introductionmentioning

confidence: 99%

“…However, most of these studies lack information on the thermodynamic characteristics of the immobilized enzyme. Only Trabizadeh et al [ 39 ] have developed full thermodynamic characteristics of naringinase from A. aculeatus , immobilized in the form of naringinase aggregates with amine groups of lysine bound to Fe 3 O 4 . However, the longest half-life of such an immobilized enzyme was just over 8 h. Therefore, it seems advisable to develop other, milder methods of immobilization of this enzyme in relation to naringinase in order to increase its thermal stability.…”

Section: Introductionmentioning

confidence: 99%

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Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Bodakowska-Boczniewicz

Garncarek

2020

Molecules

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Naringinase is an enzymatic complex used in the deglycosylation of compounds with a high application potential in the food and pharmaceutical industries. The aim of the study was to immobilize naringinase from Aspergillus niger KMS on a magnetic carrier obtained on the basis of carob gum activated by polyethyleneimine. Response surface methodology was used to optimize naringinase immobilization taking into account the following factors: pH, immobilization time, initial concentration of naringinase and immobilization temperature. The adsorption of the enzyme on a magnetic carrier was a reversible process. The binding force of naringinase was increased by crosslinking the enzyme with the carrier using dextran aldehyde. The crosslinked enzyme had better stability in an acidic environment and at a higher temperature compared to the free form. The immobilization and stabilization of naringinase by dextran aldehyde on the magnetic polysaccharide carrier lowered the activation energy, thus increasing the catalytic capacity of the investigated enzyme and increasing the activation energy of the thermal deactivation process, which confirms higher stability of the immobilized enzyme in comparison with free naringinase. The preparation of crosslinked naringinase retained over 80% of its initial activity after 10 runs of naringin hydrolysis from fresh and model grapefruit juice.

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Preparation and synthetic dye decolorization ability of magnetic cross-linked enzyme aggregates of laccase from Bacillus amyloliquefaciens

Wang

Han

Wang

et al. 2020

Bioprocess Biosyst Eng

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Nano-magnetic cross-linked enzyme aggregates of naringinase an efficient nanobiocatalyst for naringin hydrolysis

Cited by 22 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

Immobilization of Naringinase from Aspergillus Niger on a Magnetic Polysaccharide Carrier

Preparation and synthetic dye decolorization ability of magnetic cross-linked enzyme aggregates of laccase from Bacillus amyloliquefaciens

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