Xylanase Immobilized on Novel Multifunctional Hyperbranched Polyglycerol-Grafted Magnetic Nanoparticles: An Efficient and Robust Biocatalyst

Landarani‐Isfahani, Amir; Taheri‐Kafrani, Asghar; Amini, Mina; Mirkhani, Valiollah; Moghadam, Majid; Soozanipour, Asieh; Razmjou, Amir

doi:10.1021/acs.langmuir.5b02004

Cited by 86 publications

(27 citation statements)

References 60 publications

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“…The enhancement of the storage stability could be due to the physical contacts of charged residues by the interaction involving the enzyme and matrix [31,38]. The results are agreement with previous reports [38][39][40].…”

Section: Enzyme Characterizationsupporting

confidence: 92%

Immobilization and Biochemical Properties of Purified Xylanase from Bacillus amyloliquefaciens SK-3 and Its Application in Kraft Pulp Biobleaching

Kumar¹,

Haq²,

Yadav³

et al. 2016

J Clin Microbiol Biochem Technol

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In the present study, we studied the production and immobilization xylanase from Bacillus amyloliquefaciens strain SK-3. Isolate produced highest xylanase activity (56.2±1.6 IU/mol) at pH=8 and 40°C after 48 h incubation in presence of 1% wheat bran. Immobilization studies of purifi ed xylanase showed that 3.0% sodium alginate and 0.2 M calcium chloride was found to be optimum. Characterization of immobilized beads by SEM and FTIR showed signifi cant changes on the surface morphology and structure. The immobilization increases the time reaction for xylan degradation from 15-30 min and pH activity 8.0 to 9.0 whereas temperature 60-70°C with reference to free enzyme. After immobilization, thermostability of enzyme increased and retained more than 70% of its original activity after 5 h at 50°C as compared with free enzyme which showed only 20% of residual activity. Also, immobilized enzyme showed better storage stability and reusability. Overall performance of immobilized enzyme has attractive biochemical properties that make it a potential promising candidate for application in the kraft pulp pretreatment.

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Section: Enzyme Characterizationsupporting

confidence: 92%

Immobilization and Biochemical Properties of Purified Xylanase from Bacillus amyloliquefaciens SK-3 and Its Application in Kraft Pulp Biobleaching

Kumar¹,

Haq²,

Yadav³

et al. 2016

J Clin Microbiol Biochem Technol

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show abstract

“…These findings could be explained by steric effects that lead to blocking of enzymatic active sites after immobilization. Moreover, some conformational changes in the enzyme structure may occur during immobilization and may provide an additional explanation of the decrease in catalytic activity [59]. Obtained results stay in agreement with the results for catalytic activity retention (see Figure 7b).…”

Section: Kinetic Parameterssupporting

confidence: 87%

Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

et al. 2017

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The main purpose of the study was to achieve effective immobilization of lipase B from Candida antarctica (CALB) onto 3D spongin-based scaffolds from Hippospongia communis marine demosponge for rapeseed oil transesterification. Successful immobilization onto the marine sponge skeleton was confirmed for the first time. Lipase B-containing biocatalytic system exhibited the highest catalytic activity retention (89%) after 60 min of immobilization at pH 7 and temperature of 4 • C. Immobilization was found to improve the thermal and chemical stability compared to free lipase, and retain over 80% of its initial catalytic activity over a wide range of temperature (30-60 • C) and pH (6-9). Additionally, immobilized lipase has good storage stability and retains over 70% of its initial activity even after catalyzing of 25 reaction cycles. The obtained product was used in a transesterification reaction of rapeseed oil with methanol and proved to be an efficient biocatalyst for biofuel production. The highest conversion value and fatty acids methyl esters (FAME) concentration were observed after a process conducted at 40 • C and pH 10. The possible mechanism of interaction between the enzyme and the spongin-based support is proposed and discussed.

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“…xylan degradation, immobilization of xylanase has been investigated onto varied supports, such as multi-walled carbon nanotubes [11], synthesized polymer [12], nanoporous gold [13], and resin [14]. Recently, the use of magnetic nanoparticles as supports are of particular interest because they possess both the advantages of the simple separation process of magnetic materials and the high surface area and mass transfer resistance of nanosized materials [15][16][17][18][19]. An increased thermal and pH stability and good reusability of the insoluble form of the enzyme was observed in all the studies compared with the corresponding soluble enzymes.…”

mentioning

confidence: 99%

Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase

Jia

Budinova

Takasugi

et al. 2016

Biochemical Engineering Journal

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Effective degradation of hemicellulose is of utmost importance in a wide variety of applications in bioindustry. Five endoxylanases from different glycoside hydrolase families and microorganisms were tested with an arabinofuranosidase, Araf51A, for the hydrolysis of insoluble wheat arabinoxylan, which is a structural component of hemicellulose. The optimized combination was XynZ/Xyn11A/Araf51A with a loading ratio of 2:2:1, and the value of degree of synergy increased with the increase of Araf51A proportion in the enzyme mixture. Afterwards, selected enzymes were immobilized on commercial magnetic nanoparticles through covalent bonding. Both free and immobilized enzymes showed a similar conversion to reducing sugars after hydrolysis for 48 h. After 10 cycles, approximately 20% of the initial enzymatic activity of both the individual or mixture of immobilized enzymes was retained. A 5.5-fold increase in the production of sugars was obtained with a mixture of enzymes immobilized after 10 cycles in total compared with free enzymes. Importantly, a sustainable synergism between immobilized arabinofuranosidase and immobilized endoxylanases in the hydrolysis of arabinoxylan was demonstrated.

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Xylanase Immobilized on Novel Multifunctional Hyperbranched Polyglycerol-Grafted Magnetic Nanoparticles: An Efficient and Robust Biocatalyst

Cited by 86 publications

References 60 publications

Immobilization and Biochemical Properties of Purified Xylanase from Bacillus amyloliquefaciens SK-3 and Its Application in Kraft Pulp Biobleaching

Immobilization and Biochemical Properties of Purified Xylanase from Bacillus amyloliquefaciens SK-3 and Its Application in Kraft Pulp Biobleaching

Spongin-Based Scaffolds from Hippospongia communis Demosponge as an Effective Support for Lipase Immobilization

Synergistic degradation of arabinoxylan by free and immobilized xylanases and arabinofuranosidase

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