Covalent immobilization of xylanase on glutaraldehyde activated alginate beads using response surface methodology: Characterization of immobilized enzyme

Pal, Ajay; Khanum, Farhath

doi:10.1016/j.procbio.2011.02.024

Cited by 155 publications

(92 citation statements)

References 27 publications

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“…Xylanase, both free and immobilized, displayed good stability over the pH range from 3.0 to 8.0 and there was no significant differences between the adsorbed, reticulated and free xylanases as a function of pH. The same fact was observed by Pal and Khanum that reported that xylanase covalently immobilized on glutaraldehyde-alginate beads displayed behavior identical to that of the native enzyme at the same pH values [25].…”

Section: Discussionsupporting

confidence: 79%

Immobilization of Commercial Cellulase and Xylanase by Different Methods Using Two Polymeric Supports

Romo-Sánchez¹,

Camacho²,

Ramírez³

et al. 2014

ABB

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Industrial applications require enzymes highly stable and economically viable in terms of reusability. Enzyme immobilization is an exciting alternative to improve the stability of enzymatic processes. The immobilization of two commercial enzymes is reported here (cellulase and xylanase) using three chemical methods (adsorption, reticulation, and crosslinking-adsorption) and two polymeric supports (alginate-chitin and chitosan-chitin). The optimal pH for binding was 4.5 for cellulase and 5.0 for xylanase, and the optimal enzyme concentrations were 170 µg/mL and 127.5 µg/mL respectively, being the chitosan and the ideal support. In some cases, a low concentration of crosslinking agent (glutaraldehyde) improved stability of the immobilization process. Biotechnological characterization showed that the reusability of enzymes was the most striking finding, particularly of immobilized cellulase using glutaraldehyde, which after 19 cycles retained 64% activity. These results confirm the economic and biotechnical advantages of enzyme immobilization for a range of industrial applications.

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Section: Discussionsupporting

confidence: 79%

Immobilization of Commercial Cellulase and Xylanase by Different Methods Using Two Polymeric Supports

Romo-Sánchez¹,

Camacho²,

Ramírez³

et al. 2014

ABB

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“…The optimum temperatures of free and the immobilized enzyme were taken as 60 to 65 °C, respectively as maximum enzyme activity was observed at these temperatures. A similar increase in optimum temperature for immobilized xylanase was reported by other researchers [4,5,16] and this could be due to enhanced stability or conformational rigidity on immobilization. although, the effect of temperature may vary depending on the substance from which the matrix used for immobilization is made of .…”

Section: Effect Of Temperature On Immobilized Xylanasesupporting

confidence: 85%

“…In combination with enzymes like lipase and amylase, xylanases have also been used in biological deinking of paper. As the ability of enzyme to work properly at higher temperature become a common desirable property of enzymes for many industries , there has been an increasing focus on thermostable acidophilic xylanases in combination with pectinase and cellulase for their usage in juice clarification and improved yield [5]. Cloudiness in tomato fruit juice is due to formation of a colloidal suspension where the continuous medium is a solution of sugars, pectin, malic acid, and xylan, and the dispersed particles are mainly produced by cellular tissue comminuted at the time of fruit processing.…”

Section: Introductionmentioning

confidence: 99%

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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“…Immobilized enzymes are advantageous over free enzymes, as they can be recycled, reused, and save production costs at the industrial level by providing a broad spectrum of applications under different conditions (Pal and Khanum 2011b). The stabilizing effect of additives has been attributed to their ability to counteract the forces that lead to the denaturation of enzymes and loss of activity (Hall et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Thermal Stability and Thermodynamics of Xylanase from Melanocarpus albomyces in Presence of Polyols and Salts

Gupta¹,

Sahai²,

Gupta³

2014

BioResources

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An extracellular xylanase from the thermophilic fungus Melanocarpus albomyces IIS 68 was evaluated for its activity and stability in the presence of polyols and salts at 60 °C, and found to be an effective protecting agent for thermal deactivation of enzyme. Response surface methodology was employed to study the synergistic effects of glycerol and NaCl (thermostabilizers) for xylanase stability. The addition of these thermo-stabilizers resulted in more than a 10-fold increment in enzyme half-life. Activation energy (Ea) and thermodynamic parameters such as ∆H, ∆G, and ∆S were calculated for the thermal inactivation of free and immobilized xylanase. The immobilized enzyme underwent substantially less conformational changes because of its enhanced stability and increased compactness, providing better thermo-stability at elevated temperatures. These findings suggest that the combined effect of glycerol and sodium chloride serves as a potential stabilizer for extracellular thermophilic xylanase, which finds commercial application in many industries, especially in the pulp and paper industry.

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Covalent immobilization of xylanase on glutaraldehyde activated alginate beads using response surface methodology: Characterization of immobilized enzyme

Cited by 155 publications

References 27 publications

Immobilization of Commercial Cellulase and Xylanase by Different Methods Using Two Polymeric Supports

Immobilization of Commercial Cellulase and Xylanase by Different Methods Using Two Polymeric Supports

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

Thermal Stability and Thermodynamics of Xylanase from Melanocarpus albomyces in Presence of Polyols and Salts

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