Xylanase immobilization on magnetite and magnetite core/shell nanocomposites using two different flexible alkyl length organophosphonates: Linker length and shell effect on enzyme catalytic activity

Singh, Vishal; Kaul, Sunaina; Singla, Prinka; Kumar, Vinod; Sandhir, Rajat; Chung, Jong Hoon; Garg, Pankaj; Singhal, Nitin

doi:10.1016/j.ijbiomac.2018.04.097

Cited by 28 publications

(22 citation statements)

References 39 publications

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“…The larger moiety namely cellulase conjugated in the present work may be better at amplifying differences in the linker length-associated surface coverage on nanoparticles. Activity of xylanase immobilized on magnetite nanoparticles have been previously reported to vary significantly with linker length [44]. Chitosan coated magnetic nanoparticles (C5-C-IOMNPs) exhibit the highest loading efficiency (92%) while C5-SNPs and C5-S-IOMNPs display enzyme loading of 74% and 67%, respectively (Fig.…”

Section: Resultsmentioning

confidence: 97%

Investigation of nanoparticle immobilized cellulase: nanoparticle identity, linker length and polyphenol hydrolysis

Kumar

Morya

Gadhavi

et al. 2019

Heliyon

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Cellulase containing nanobiocatalysts have been useful as an extraction tool based on their ability to disrupt plant cell walls. In this work, we investigate the effect of nanoparticle composition and chemical linkage towards immobilized cellulase activity. Cellulase nanoconstructs have been prepared, characterized and compared for their loading efficiencies with standard assays and enzyme kinetics and correlate well with the cognate loading efficiencies. Application of the cellulase-immobilized nanoparticles on onion skins results in release of a distinctive composition of polyphenols. The aglycosidic form of quercetin is the dominant product of onion skin hydrolysis affected by cellulase nanobiocatalysts. Chitosan-coated iron oxide nanoparticles with APTES-conjugated cellulase are found to be most effective for polyphenol release and for transformation of glycosidic to aglycosidic form of quercetin. These results shed light on the activity of immobilized cellulase beyond their role in cell wall disruption and are important for the practical application of cellulase nanobiocatalysts.

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Section: Resultsmentioning

confidence: 97%

Investigation of nanoparticle immobilized cellulase: nanoparticle identity, linker length and polyphenol hydrolysis

Kumar

Morya

Gadhavi

et al. 2019

Heliyon

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“…Next, we measured the enzyme activity at the temperature range from 30 to 90 • C. Figure 5c reveals that the relative activity of the immobilized enzyme was better than that of the free enzyme at the various temperatures, with the optimal reaction temperature of the immobilized enzyme at 80 • C; the free enzyme revealed its best activity at 70 • C. Previous reports have indicated that the optimal reaction temperature of xylanase free enzyme derived from Aspergillus terreus falls between 60 and 70 • C [32], whereas, the optimal reaction temperature of most xylanases was set between 30 and 60 • C [27,35,36]; furthermore, immobilization of xylanase from Thermomyces lanuginosus increased its optimal reaction temperature [27]. Therefore, it appears reasonable that 80 • C would be the optimal reaction temperature in this present study.…”

Section: Characteristics Of the Immobilized Enzymementioning

confidence: 90%

“…Santos et al immobilized xylanase in poly(vinyl alcohol) fibers, resulting in a high hydrolysis rate of 406.7 µM/min at pH 6 and 70 • C [26]. Singh et al immobilized xylanase on synthesized silica-coated magnetite nanoparticles through ethyl carbodiimide coupling; the covalently bonded immobilized enzyme retained 90% of its activity after undergoing 10 reaction cycles [27].…”

Section: Introductionmentioning

confidence: 99%

Co-Immobilization of Xylanase and Scaffolding Protein onto an Immobilized Metal Ion Affinity Membrane

Wong

Juang

et al. 2020

Catalysts

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Lignocellulosic biomass conversion technology seeks to convert agricultural waste to sugars through the use of various cellulases and hemicellulases. In practice, the application of free enzymes might increase the cost of the process due to difficulties with recovery of the enzymes and products. Immobilization might be an effective approach for recovering the hydrolysis products and improving the stability and reusability of the enzymes. In this study, we used a recombinant genetic engineering approach to construct a scaffold protein gene (CipA) and a xylanase gene (XynC) fused to a dockerin gene (DocT). After expressing CipA and XynC-DocT (XynCt) genes using E. coli hosts, the crude extracts were collected. An immobilized metal ion affinity membrane/Co2+ ion (IMAM-Co2+) system was prepared to adsorb CipA in its crude extract, thereby allowing simultaneous purification and immobilization of CipA protein. A similar approach was applied for the adsorption of XynCt protein, exploiting the interaction between the cohesin units in IMAM-Co2+-CipA and the dockerin unit in XynCt. The activity of the xylanase unit was enhanced in the presence of Co2+ for both the free XynCt enzymes and the immobilized CipA-XynCt. The heat resistance and stability over a wide range of values of pH of the immobilized CipA-XynCt were superior to those of the free XynCt. Furthermore, the immobilized CipA-XynCt retained approximately 80% of its initial activity after seven reaction cycles. The values of Km and νmax of IMAM-Co2+-CipA-XynCt (1.513 mg/mL and 3.831 U/mg, respectively) were the best among those of the other tested forms of XynCt.

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“…These results are in agreement with the previously reported K M values for the enzymatic hydrolysis reaction using a xylanase (EC 3.2.1.8) from Thermomyces lanuginosus (powder, ≥2500 units g −1 of the protein), where K M values were in the range between 4.01 32 and 9.41 mg mL −1 . 33 However, in the cited studies, different substrates (beech wood and birch wood xylan) were used compared to this work. For experiments with the biofunctionalized MNPs, the amount of immobilized enzyme (0.42 ± 0.02 mg mg MNP −1 ) was higher than that reported by other authors (0.28 32 and 0.22 mg mg MNP −122 ) although they used particles with a smaller diameter (9 and 8 nm vs 200 nm in this work).…”

Section: Equipment and Experimental Proceduresmentioning

confidence: 99%

Enzymatic Hydrolysis of Xylan from Coffee Parchment in Membrane Bioreactors

Fernández

Poerio

Nabarlatz

et al. 2020

Ind. Eng. Chem. Res.

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Xylooligosaccharides (XOs) production from xylan, extracted from coffee parchment, using two stirred tank reactors (STRs) and two membrane bioreactors (MBRs) was studied for the first time. In the reactors, xylanase either free in a solution (E-STR, E-MBR) or covalently immobilized on magnetic nanoparticles (MNP-STR, MNP-MBR) was used. A continuous production of reducing sugars in both MBRs was obtained. In the E-MBR, the same conversion of E-STR at a low substrate concentration (1 mg mL −1 ) (97%) was obtained. At higher substrate concentration, the conversion increases by a quarter in E-MBR on increasing the residence time and doubles in MNP-MBR by increasing the amount of immobilized enzyme. The unchanged apparent K M (about 8 mg mL −1 ) showed that the affinity of the enzyme for the substrate was not altered by the immobilization process. In E-MBR, the enzyme/substrate affinity is even improved (K M : 2.58 mg mL −1 ), thanks to the continuous removal of the inhibition products, present in the initial xylan solution, by the membrane process.

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Xylanase immobilization on magnetite and magnetite core/shell nanocomposites using two different flexible alkyl length organophosphonates: Linker length and shell effect on enzyme catalytic activity

Cited by 28 publications

References 39 publications

Investigation of nanoparticle immobilized cellulase: nanoparticle identity, linker length and polyphenol hydrolysis

Investigation of nanoparticle immobilized cellulase: nanoparticle identity, linker length and polyphenol hydrolysis

Co-Immobilization of Xylanase and Scaffolding Protein onto an Immobilized Metal Ion Affinity Membrane

Enzymatic Hydrolysis of Xylan from Coffee Parchment in Membrane Bioreactors

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