Properties of Aspergillus subolivaceus free and immobilized dextranase

El-Tanash, A. B.; El-Baz, E. E. T.; Sherief, A.A.

doi:10.1007/s00217-011-1570-1

Cited by 27 publications

(12 citation statements)

References 31 publications

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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: 74%

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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Section: Effect Of Ph and Temperature On Enzyme Activitysupporting

confidence: 74%

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 shift in pH mostly depends on the pH of micro-environment around the immobilized enzyme and also the physico-chemical nature of support material contributes up to some extent. Similar findings were observed for immobilized phospholipase A1 in gelatin hydrogel [ 29 ], naringinase in PVA matrices [ 30 ], laccase in PVA cryo-gel carrier [ 31 ] and dextranase in bovine serum albumin [ 32 ].…”

Section: Resultssupporting

confidence: 74%

Sandal reactive dyes decolorization and cytotoxicity reduction using manganese peroxidase immobilized onto polyvinyl alcohol-alginate beads

Bilal

Asgher

2015

Chemistry Central Journal

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BackgroundFungal manganese peroxidases (MnPs) have great potential as bio-remediating agents and can be used continuously in the immobilized form like many other enzymes.ResultsIn the present study, purified manganese peroxidase (MnP) enzyme isolated from Ganoderma lucidum IBL-05 was immobilized onto polyvinyl alcohol-alginate beads and investigated its potential for the decolorization and detoxification of new class of reactive dyes and textile wastewater. The optimal conditions for MnP immobilization were 10 % (w/v) PVA, 1.5 % sodium alginate, 3 % boric acid and 2 % CaCl2 solution. The optimum pH, temperature and kinetic parameters (Km and Vmax) for free and immobilized MnP were found to be significantly altered after immobilization. The immobilized MnP showed high decolorization efficiency for Sandal reactive dyes (78.14–92.29 %) and textile wastewater (61–80 %). Reusability studies showed that after six consecutive dye decolorization cycles, the PVA coupled MnP retained more than 60 % of its initial activity (64.9 % after 6th cycle form 92.29 % in 1st cycle) for Sandal-fix Foron Blue E2BLN dye. The water quality assurance parameters (BOD, COD and TOC) and cytotoxicity (haemolytic and brine shrimp lethality tests) studies before and after treatment were employed and results revealed that both the dyes aqueous solution and textile wastewater were cytotoxic that reduced significantly after treatment.ConclusionsThe decolorization and cytotoxicity outcomes indicated that immobilized MnP in PVA–alginate beads can be efficiently exploited for industrial and environmental applications, especially for remediation of textile dyes containing wastewater effluents. Graphical abstractDye decolorizing potential of immobilized MnP

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“…However, the V max value of dextranase decreased after entrapment into the spheres with a calculated value of 4732 μmol ml -1 with a standard error of 90.34, and the K m value of entrapped dextranase varied from the value of its soluble counterpart with a twofold increase of 9.466 mg ml -1 having a standard error of 0.654. The same phenomenon after immobilization was also reported by El-Tanash, and the reason suggested for the increased K m value was the low availability of the substrate for the active site of immobilized dextranase while a decrease in velocity of reaction represented a decrease in flexibility of dextranase after entrapment [26]. Previously, it was also reported by another author that entrapment did not cause a pronounced effect on the kinetic characteristics of the enzyme [27].…”

Section: Enzyme Kineticssupporting

confidence: 77%

Immobilization of Dextranase Using Anionic Natural Polymer Alginate as a Matrix for the Degradation of a Long-Chain Biopolymer (Dextran)

Shahid

Aman

Qader

2019

International Journal of Polymer Science

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Alginate is an inexpensive, nontoxic, valuable biopolymer utilized in the study for the immobilization of commercially applicable biocatalyst dextranase. Dextranase was immobilized by an entrapment method, and alginate hydrogel spheres were synthesized after optimizing several parameters. A sodium alginate concentration of 4.0% was noticed to be suitable along with a calcium chloride concentration of 0.2 molar after providing a curing time of 20 minutes. After comparing the characteristics of the entrapped enzyme with those of the soluble one, it was observed that the characteristics were more or less the same except for the change in reaction time which was noticed to be prolonged in the case of entrapped dextranase while the change in temperature and pH optima was not observed. The variation in Vmax and Km values of dextranase after entrapment was also noted. However, after extensive stability examination studies, it was found that dextranase became more stable after entrapment; as a result, it retained more than 50% of its original activity at elevated temperature even after exposure for about 2.0 hours. The reusability of dextranase was up to 7.0 cycles after performing catalytic activity under constant condition.

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Properties of Aspergillus subolivaceus free and immobilized dextranase

Cited by 27 publications

References 31 publications

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

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

Sandal reactive dyes decolorization and cytotoxicity reduction using manganese peroxidase immobilized onto polyvinyl alcohol-alginate beads

Immobilization of Dextranase Using Anionic Natural Polymer Alginate as a Matrix for the Degradation of a Long-Chain Biopolymer (Dextran)

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