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Norouzian, Dariush; Hosseinzadeh, A.; Inanlou, Davoud Nouri; Moazami, Nader

doi:10.1023/a:1008980018481

Cited by 24 publications

(11 citation statements)

References 6 publications

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“…The optimum temperature values reported from previous studies, for free naringinase, from P. decumbens showed values of 55°C [45], 70°C [43,44], and 60°C [45] from A. niger naringinase.…”

Section: Free Immobilizedmentioning

confidence: 66%

“…Also, optimum pH values of 4.5 for naringinase from A. niger [43] and from P. decumbens [44] were referred. Lower pH values were reported for immobilized naringinase from P. decumbens, like 3.5 on Celite by the adsorption/cross-link with glutaraldehyde [45] and on activated seeds of Ocimum basilicum with covalent binding method [46]. Tsen et al [47] referred an optimum pH value of 3.7 from Penicillium sp.…”

Section: Effect Of Ph On the Activity Of Free And Immobilized Naringimentioning

confidence: 99%

“…In previous studies on the immobilization of naringinase from P. decumbens, an optimum temperature of 60°C was reported, with entrapment in gelatin open-pore matrix and in calcium alginate beads [45], with adsorption/covalent binding method with glutaraldehyde in Celite [44] and with covalent binding in hen egg white [45]. When naringinase from Penicillium sp.…”

Section: Free Immobilizedmentioning

confidence: 99%

“…When naringinase from Penicillium sp. was entrapped in cellulose triacetate fiber [46], an optimum temperature of 55°C was reported. An optimum temperature of 65°C was reported for naringinase immobilized in activated seeds of O. basilicum [47], while 70°C was referred for naringinase from A. niger immobilized in PVA cryogel with freeze and thawing method [42].…”

Section: Free Immobilizedmentioning

confidence: 99%

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Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

Nunes

Vila-Real

Fernandes

et al. 2009

Appl Biochem Biotechnol

101

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A synthetic polymer, polyvinyl alcohol (PVA), a cheap and nontoxic synthetic polymer to organism, has been ascribed for biocatalyst immobilization. In this work PVA-alginate beads were developed with thermal, mechanical, and chemical stability to high temperatures (<80 degrees C). The combination of alginate and bead treatment with sodium sulfate not only prevented agglomeration but produced beads of high gel strength and conferred enzyme protection from inactivation by boric acid. Naringinase from Penicillium decumbens was immobilized in PVA (10%)-alginate beads with three different sizes (1-3 mm), at three different alginate concentrations (0.2-1.0%), and these features were investigated in terms of swelling ratio within the beads, enzyme activity, and immobilization yield during hydrolysis of naringin. The pH and temperature optimum were 4.0 and 70 degrees C for the PVA-alginate-immobilized naringinase. The highest naringinase activity yield in PVA (10%)-alginate (1%) beads of 2 mm was 80%, at pH 4.0 and 70 degrees C. The Michaelis constant (K(Mapp)) and the maximum reaction velocity (V(maxapp)) were evaluated for both free (K(Mapp) = 0.233 mM; V(maxapp) = 0.13 mM min(-1)) and immobilized naringinase (K(Mapp) = 0.349 mM; V(maxapp) = 0.08 mM min(-1)). The residual activity of the immobilized enzyme was followed in eight consecutive batch runs with a retention activity of 70%. After 6 weeks, upon storage in acetate buffer pH 4 at 4 degrees C, the immobilized biocatalyst retained 90% of the initial activity. These promising results are illustrative of the potential of this immobilization strategy for the system evaluated and suggest that its application may be effectively performed for the entrapment of other biocatalysts.

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Section: Free Immobilizedmentioning

confidence: 66%

Section: Effect Of Ph On the Activity Of Free And Immobilized Naringimentioning

confidence: 99%

Section: Free Immobilizedmentioning

confidence: 99%

Section: Free Immobilizedmentioning

confidence: 99%

See 2 more Smart Citations

Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

Nunes

Vila-Real

Fernandes

et al. 2009

Appl Biochem Biotechnol

101

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“…α-L-Rhamnosidase from Penicillium decumbens is an extracellular glycoprotein (50% glycosidation grade) of 90 kDa showing optimal activity at pH 3.5-4.5 and 57°C [3,17]. In contrast to the other fungal α-L-rhamnosidases, less information is published about its stability profiles of the free form, and most studies deal with stabilities in immobilized state [18][19][20][21].…”

Section: Introductionmentioning

confidence: 99%

Deactivation Kinetics and Response Surface Analysis of the Stability of α-l-Rhamnosidase from Penicillium decumbens

Magario

Neumann

Oliveros

et al. 2008

Appl Biochem Biotechnol

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The stability of the mixed enzyme preparation Naringinase from Penicillium decumbens was studied in dependence of the temperature, the pH value, and the enzyme concentration by means of response surface methodology. Deactivation kinetics by formation of an intermediate state was proposed for fitting deactivation data. Empirical models could then be constructed for prediction of deactivation rate constants, specific activity of intermediate state, and half-life values under different incubation conditions. From this study, it can be concluded that (1) Naringinase is most stable in the pH range of 4.5-5.0, being quite sensitive to lower pHs (<3.5) and (2) the glyco-enzyme is a rather thermo-stable enzyme preserving its initial activity for long times when incubated at its optimal pH up to temperatures of 65 degrees C. Enriched alpha-L-rhamnosidase after column treatment and ultrafiltration presented similar deactivation kinetics pattern and half-life values as the unpurified enzyme. Thus, any influence of low molecular weight substances on its deactivation is most probably negligible. The intermediate state of the enzyme may correspond to unfolding and self-digestion of its carbohydrate portion, lowering its activity relative to the initial state. The digestion- and unfolding-grade of this intermediate state may also be controlled by the pH and temperature of incubation.

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Covalent Immobilization of Naringinase over Two‐Dimensional 2D Zeolites and its Applications in a Continuous Process to Produce Citrus Flavonoids and for Debittering of Juices

et al. 2020

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The crude naringinase from Penicillium decumbens and a purified naringinase with high α‐L‐rhamnosidase activity could be covalently immobilized on two‐dimensional zeolite ITQ‐2 after surface modification with glutaraldehyde. The influence of pH and temperature on the enzyme activity (in free and immobilized forms) as well as the thermal stability were determined using the specific substrate: p‐nitrophenyl‐alpha‐L‐rhamnopyranoside (Rha‐pNP). The crude and purified naringinase supported on ITQ‐2 were applied in the hydrolysis of naringin, giving the flavonoids naringenin and prunin respectively with a conversion >90 % and excellent selectivity. The supported enzymes showed long term stability, being possible to perform up to 25 consecutive cycles without loss of activity, showing its high potential to produce the valuable citrus flavonoids prunin and naringenin. We have also succeeded in the application of the immobilized crude naringinase on ITQ‐2 for debittering grapefruit juices in a continuous process that was maintained operating for 300 h, with excellent results.

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Untitled

Cited by 24 publications

References 6 publications

Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

Immobilization of Naringinase in PVA–Alginate Matrix Using an Innovative Technique

Deactivation Kinetics and Response Surface Analysis of the Stability of α-l-Rhamnosidase from Penicillium decumbens

Covalent Immobilization of Naringinase over Two‐Dimensional 2D Zeolites and its Applications in a Continuous Process to Produce Citrus Flavonoids and for Debittering of Juices

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