Immobilization and characterization of naringinase for the hydrolysis of naringin

Şekeroğlu, Gülten; Fadı́loğlu, Sibel; Göğüş, Fahrettin

doi:10.1007/s00217-006-0288-y

Cited by 32 publications

(23 citation statements)

References 24 publications

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“…The degree of naringin hydrolysis was linearly proportional to the enzyme concentration up to 2,000 mg L −1 . These results were similar to that reported by Sekeroglu et al [39] for the same enzyme but using different immobilization method, although, in Pedro et al [40] and Ribeiro et al [41], linear proportionality was attained for enzyme concentrations below 500 mg L −1 with naringinase immobilized, respectively, on calcium alginate (2%) and K-carrageenan (2%) beads. The naringinase concentration used in further experiments was 2,000 mg L −1 relative to the reaction media for both free and immobilized enzyme.…”

Section: Effect Of Different Concentrations Of Enzyme On Activitysupporting

confidence: 90%

“…Similar observations has been frequently reported in the literature [5], namely in the work of Sekeroglu et al [39], with naringinase from P. decumbens, and of Busto et al [42], with naringinase from Aspergillus niger for free and immobilized forms, in PVA cryogel. Also, optimum pH values of 4.5 for naringinase from A. niger [43] and from P. decumbens [44] were referred.…”

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

confidence: 89%

“…At standard reaction conditions of 30°C and pH 4.0, the activity retention was 65%. When naringinase was used for immobilization in Ca-alginate beads under 0.1 and 160 MPa, a residual activity of 35% and 70%, respectively, was obtained [39]. A residual activity of 57% was referred at optimum conditions of 65°C and pH 3.5, with naringinase immobilized on activated seeds of O. basilicum [47].…”

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

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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: Effect Of Different Concentrations Of Enzyme On Activitysupporting

confidence: 90%

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

confidence: 89%

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

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“…It was also observed that high activity of the immobilized enzyme occurred in a broad pH between 5.2-6.4, which implied that the beads played a protective role for the immobilized enzyme. Similar results were reported for free phospholipase A1 in gelatin hydrogel (Sheelu et al, 2008), free naringinase in PVA matrices (Şekeroğlu et al, 2006;Nunes et al, 2010), laccase in PVA Cryogel Type Carrier (Stanescu et al, 2010) and dextranase in BSA with a cross-linking agent (El-Tanash et al, 2011).…”

Section: Effect Of Ph and Temperature On Enzyme Activitysupporting

confidence: 86%

Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization

Zhan

Jiang

Pan

2013

Braz. J. Chem. Eng.

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-The paper presents the synthesis and performance of an immobilized phospholipase A1 with practical application for oil degumming. The polyvinyl alcohol (PVA) had a number of properties indicating this polymer as a good enzyme carrier. The combination with alginate made a macro-porous structure, evidenced by SEM analyses. When the process time in boric acid solution was 30 minutes, the results revealed that beads prepared with 10% (w/v) PVA and 2% (w/v) sodium alginate in 4% (w/v) boric acid and 2% (w/v) calcium chloride solution exhibited high immobilized enzyme activity, immobilization yield and stability. The pH and temperature optimum for the PVA-alginate immobilized phospholipase A1were 5.6 and 58 °C, respectively. The enzyme immobilized in the beads retained 50.37% of the initial activity in the eighth cycle. The enzyme biocatalyst immobilized in the beads retained 78.58% of the initial activity after storing 6 weeks at 4 °C.

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“…It has been already clarified that a-L-rhamnosidase hydrolyzes naringin (4, 5, 7-trihydroxyflavanone-7-rhamnoglucoside) into prunin (4, 5, 7-trihydroxyflavanone-7-glucoside) which is then converted by b-D-glucosidase to naringenin (4, 5, 7-trihydroxy-flavonone) (Sekeroglu et al 2006).…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of a new naringinase-producing strain, Williopsis californica Jmudeb007

Xiao

et al. 2011

World J Microbiol Biotechnol

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A new naringinase-producing strain, Jmudeb007 was indentified by means of morphological observation, gene homogeneous analysis and physiological and biochemical test. Its characteristics in expressing naringinase were investigated by batch culture in 7 L fermentors. Jmudeb007 grown white, circular, convex, and smooth edged colonies, and single, oval-shaped and nucleus contained cells. Its gene sequences of 26S rDNA D1/D2 region and 5.8S rDNA-ITS region both showed homogeneities at 99% to Williopsis californica. It appeared positive in glucose fermentation test, negative in urease test and diazo blue B (DBB) test. Strain Jmudeb007 was identified to W. californica. Cultivation of Jmudeb007 with three media containing different amount of glucose showed it was capable of expressing naringinase which hydrolyze naringin to naringenin. The naringinase synthesis of Jmudeb007 was regulated by glucose which depended on the concentration. Jumdeb007 could express naringinase in medium containing glucose no more than 4 g/L. The present work provides a new source of naringinase, W. californica Jmudeb007, which is non-pathogenic, convenient to conduct breeding operation, easy to develop fermentation process. It is the first report about yeast that can produce naringinase, which help to explore naringinase and other glycosidase from yeast.

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Immobilization and characterization of naringinase for the hydrolysis of naringin

Cited by 32 publications

References 24 publications

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

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

Immobilization of phospholipase a1 using a polyvinyl alcohol-alginate matrix and evaluation of the effects of immobilization

Identification and characterization of a new naringinase-producing strain, Williopsis californica Jmudeb007

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