Improved enzyme properties upon glutaraldehyde cross-linking of alginate entrapped xylanase from Bacillus licheniformis

Kumar, Sumit; Haq, Izharul; Prakash, Jyoti; Raj, Abhay

doi:10.1016/j.ijbiomac.2017.01.104

Cited by 78 publications

(36 citation statements)

References 37 publications

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“…Figure 3a shows the results of the investigation of the dependence of pH on the activity of both the free as well as immobilized enzymes, which was performed within the pH range of pH 3-pH 8 at room temperature while setting the highest activity at 100%. Immobilization of enzymes onto charged supports is normally the reason for the deviations of the pH-activity profile to either high or low pH regions [46,47]. The results from this study have indicated that there was no difference in terms of the profile of pH-activity between the free and the immobilized laccase at an optimum pH of 5, although the immobilized laccase showed better adaptability in a wider pH region compared to the free laccase.…”

Section: Estimation Of Kinetic Parameters For the Free Enzyme Laccasementioning

confidence: 61%

“…As for Vmax, a value of 2.9 mM min −1 was recorded for the free laccase, which decreased 1.4 mM min −1 upon immobilization. This trend, which resulted in the increase of Km and decrease of Vmax after the immobilization, might have been caused by the steric hindrances on the active site of the enzyme caused by the introduction of the support [47]. Figure 3a shows the results of the investigation of the dependence of pH on the activity of both the free as well as immobilized enzymes, which was performed within the pH range of pH 3-pH 8 at room temperature while setting the highest activity at 100%.…”

Section: Estimation Of Kinetic Parameters For the Free Enzyme Laccasementioning

confidence: 99%

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Laccase Immobilized Fe3O4-Graphene Oxide Nanobiocatalyst Improves Stability and Immobilization Efficiency in the Green Preparation of Sulfa Drugs

et al. 2020

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This paper, reports on the novel and green synthesis procedure for sulfonamides that involved the immobilization of Trametes Versicolor laccase onto the Fe3O4–graphene nanocomposite via glutaraldehyde (GA) crosslinking (Lac/Fe3O4/GO). Various parameters, mainly, activation time, GA, and laccase concentration were investigated and optimized. The results showed that the optimal contact time was 4 h, GA concentration was 5% while laccase concentration was 5 mg·mL−1, at which a high enzyme activity recovery was achieved (86%). In terms of the stability of immobilized laccase to temperature and storage conditions, the performance of the nanobiocatalyst was found to significantly exceed that of free laccase. The results have indicated that nearly 70% of relative activity for immobilized laccase remained after the incubation period of 2 h at 55 °C, but only 48% of free laccase remained within the same time period. Moreover, the immobilized laccase retained 88% of its initial activity after storage for 20 days. In case of the free laccase, the activity retained within the same time period was 32%. In addition, the nanobiocatalyst possessed better recycling performance as evidenced from the observation that after eight cycles of repeated use, it retained 85% of its original activity.

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Section: Estimation Of Kinetic Parameters For the Free Enzyme Laccasementioning

confidence: 61%

Section: Estimation Of Kinetic Parameters For the Free Enzyme Laccasementioning

confidence: 99%

Laccase Immobilized Fe3O4-Graphene Oxide Nanobiocatalyst Improves Stability and Immobilization Efficiency in the Green Preparation of Sulfa Drugs

et al. 2020

View full text Add to dashboard Cite

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“…the result of which are shown in Fig 3.The residual activity of immobilized xylanase was more than 90 %, 85%, 79 % and 55 % after 1, 2, 3 and 4 response cycles, individually. The reduction in residual activity of enzyme with no of cycle has been accounted by a few scientists [11,12]. A decrease in residual activity of enzyme may happen because of inactivation of enzyme as recommended before [13].The considerable stability observed during immobilized xylanase in this study would make the process economical.…”

Section: Reusability Of Immobilized Xylanasementioning

confidence: 73%

Industrial application of glutaraldehyde activated immobilized xylanase for clarification of tomato juice

2017

Int. J. Adv. Res. Biol. Sci

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Xylanase is being utilized in many industries and fruit juice clarification is one of them. The industrial use of a free xylanase enzyme is finite because it is expensive and is structurally unbalanced in free form and not stable at high pH and temperature, which can be reduced by entrapment of xylanase upon an insoluble support. Immobilization of xylanase enzyme can be done within sodium alginate beads using entrapment technique. In this study amalgamation of sodium alginate and calcium chloride (0.44 M) was used for the preparation of immobilized beads. After the enzyme is immobilized it is applied on tomato juice which can be obtained by simple extraction .The turbidity and viscosity of juice is due the presence of polysaccharides like cellulose, hemicelluloses, starch, pectin etc. Therefore, juices needs be clarified before commercialization in market. Treatment of tomato juice with xylanase under optimized conditions resulted in an increase in reducing sugars, juice clarity, filterability, pH and but a decline in turbidity and viscosity. Immobilized xylanase was more effective in improving tomato juice overall acceptability and quality as compared to its soluble counterpart. The results showed xylanase, in immobilized form, is a potential candidate for use in fruit juice clarification. The clarity of juice is measured by comparing the transmittance of both samples that is tomato juice treated with xylanase and juice not treated with xylanase.

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“…Xylanase isolated from Aspergillus flavus and Bacillus licheniformis were subjected to entrapment in alginate beads followed by glutaraldehyde crosslinking. This not only resulted in the reduction of enzyme leaching but also showed higher stability over wide pH range, better thermal and storage stability with improved kinetic parameters …”

Section: Stabilization Of Cellulolytic Enzymesmentioning

confidence: 96%

Stable Cellulolytic Enzymes and Their Application in Hydrolysis of Lignocellulosic Biomass

2018

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The effective utilization of lignocellulosic biomass for production of valueadded products in bio-refineries mainly depends on their hydrolysis into constituent soluble sugars. Despite the commercial availability of lignocellulolytic enzymes, there are certain challenges in using them at an industrial scale which arise from their inherent characteristics. Hence, development of industrially potent and stable cellulolytic enzymes is of great importance. While a lot of emphasis has been given to produce the enzymes with high titre and productivity, the properties of these enzymes, which affect their performance in hydrolyzing lignocellulosic residues, have largely been ignored. The various properties that affect the hydrolysis are thermal stability, catalytic efficiency, non-specific adsorption, end-product inhibition resistance, and shear inactivation. This review discusses several approaches such as finding new enzymes from extremophiles, recombinant production of cellulolytic enzymes in industrial strains, directed evolution and mutagenesis, and formation of the enzyme aggregates that are being investigated to develop stable cellulase enzymes. The authors also suggest that for a meaningful information on the modified cellulolytic enzymes and their application in cellulose hydrolysis, they should be evaluated under practical process condition.

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Improved enzyme properties upon glutaraldehyde cross-linking of alginate entrapped xylanase from Bacillus licheniformis

Cited by 78 publications

References 37 publications

Laccase Immobilized Fe3O4-Graphene Oxide Nanobiocatalyst Improves Stability and Immobilization Efficiency in the Green Preparation of Sulfa Drugs

Laccase Immobilized Fe3O4-Graphene Oxide Nanobiocatalyst Improves Stability and Immobilization Efficiency in the Green Preparation of Sulfa Drugs

Industrial application of glutaraldehyde activated immobilized xylanase for clarification of tomato juice

Stable Cellulolytic Enzymes and Their Application in Hydrolysis of Lignocellulosic Biomass

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