Immobilization of xylanase on modified grafted alginate polyethyleneimine bead based on impact of sodium cation effect

Alginate- polyethyleneimine gel beads modified by using 0.3 M Na+ were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed distorted structure with addition of Na+ that impaired the egg-box structure formation offered much covalent binding with xylanase. Immobilization...

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Published inInternational journal of biological macromolecules Vol. 140; pp. 1284 - 1295
Main Authors Mostafa, Faten A., El Aty, Abeer A.A., Hassan, Mohamed E., Awad, Ghada E.A.
Format Journal Article
LanguageEnglish
Published Netherlands Elsevier B.V 01.11.2019
Subjects
Alginates - chemistry
Aspergillus flavus - enzymology
Biocatalysis
Cations
Covalent immobilization
Effect of sodium cation
Endo-1,4-beta Xylanases - metabolism
Enzyme Stability
Enzymes, Immobilized - metabolism
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Microspheres
Polyethyleneimine - chemistry
Sodium - chemistry
Spectrometry, X-Ray Emission
Spectroscopy, Fourier Transform Infrared
Temperature
Xylanase
Xylans - metabolism
Xylanase
Effect of sodium cation
Covalent immobilization
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Abstract Alginate- polyethyleneimine gel beads modified by using 0.3 M Na+ were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed distorted structure with addition of Na+ that impaired the egg-box structure formation offered much covalent binding with xylanase. Immobilization onto (Alg+PEI/Na+) showed an enhancement in the operational stability, immobilization efficiency as well as immobilization yield. Covalent immobilization of xylanase onto (Alg+PEI/Na+) enhanced xylanase activity over a wide range of pHs (4–5.5) comparable to its free formula. As well as an increase in reaction temperature up to 60°C. However, immobilized formula of enzyme showed abroad thermal stability that it retained 79.0% of its initial activity at 70°C up to 30 min whereas, free formula completely lost its activity at this temperature. Thermodynamics studies showed an enhancement in thermal stability at high temperature for the immobilized xylanase. i.e. At 70°C the t1/2 and D-value for free formula of enzyme increased from 24 to165 min and from 79.95to 548.23 min, respectively. Moreover, the enzyme stability enhancement for immobilized formula of xylanase was proved with a remarkable increase in enthalpy and free energy. 93% of the immobilized xylanase activity was retained over 6 weeks of storage at -4°C.
AbstractList Alginate- polyethyleneimine gel beads modified by using 0.3 M Na were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed distorted structure with addition of Na that impaired the egg-box structure formation offered much covalent binding with xylanase. Immobilization onto (Alg+PEI/Na ) showed an enhancement in the operational stability, immobilization efficiency as well as immobilization yield. Covalent immobilization of xylanase onto (Alg+PEI/Na ) enhanced xylanase activity over a wide range of pHs (4-5.5) comparable to its free formula. As well as an increase in reaction temperature up to 60°C. However, immobilized formula of enzyme showed abroad thermal stability that it retained 79.0% of its initial activity at 70°C up to 30 min whereas, free formula completely lost its activity at this temperature. Thermodynamics studies showed an enhancement in thermal stability at high temperature for the immobilized xylanase. i.e. At 70°C the t and D-value for free formula of enzyme increased from 24 to165 min and from 79.95to 548.23 min, respectively. Moreover, the enzyme stability enhancement for immobilized formula of xylanase was proved with a remarkable increase in enthalpy and free energy. 93% of the immobilized xylanase activity was retained over 6 weeks of storage at -4°C.
Alginate- polyethyleneimine gel beads modified by using 0.3 M Na+ were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed distorted structure with addition of Na+ that impaired the egg-box structure formation offered much covalent binding with xylanase. Immobilization onto (Alg+PEI/Na+) showed an enhancement in the operational stability, immobilization efficiency as well as immobilization yield. Covalent immobilization of xylanase onto (Alg+PEI/Na+) enhanced xylanase activity over a wide range of pHs (4–5.5) comparable to its free formula. As well as an increase in reaction temperature up to 60°C. However, immobilized formula of enzyme showed abroad thermal stability that it retained 79.0% of its initial activity at 70°C up to 30 min whereas, free formula completely lost its activity at this temperature. Thermodynamics studies showed an enhancement in thermal stability at high temperature for the immobilized xylanase. i.e. At 70°C the t1/2 and D-value for free formula of enzyme increased from 24 to165 min and from 79.95to 548.23 min, respectively. Moreover, the enzyme stability enhancement for immobilized formula of xylanase was proved with a remarkable increase in enthalpy and free energy. 93% of the immobilized xylanase activity was retained over 6 weeks of storage at -4°C.
Author Awad, Ghada E.A.
Hassan, Mohamed E.
Mostafa, Faten A.
El Aty, Abeer A.A.
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Keywords Xylanase
Effect of sodium cation
Covalent immobilization
Language English
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Snippet Alginate- polyethyleneimine gel beads modified by using 0.3 M Na+ were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed...
Alginate- polyethyleneimine gel beads modified by using 0.3 M Na were used for covalent immobilization of Aspergillus flavus xylanase. SEM images showed...
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SubjectTerms Alginates - chemistry
Aspergillus flavus - enzymology
Biocatalysis
Cations
Covalent immobilization
Effect of sodium cation
Endo-1,4-beta Xylanases - metabolism
Enzyme Stability
Enzymes, Immobilized - metabolism
Hydrogen-Ion Concentration
Hydrolysis
Kinetics
Microspheres
Polyethyleneimine - chemistry
Sodium - chemistry
Spectrometry, X-Ray Emission
Spectroscopy, Fourier Transform Infrared
Temperature
Xylanase
Xylans - metabolism
Title Immobilization of xylanase on modified grafted alginate polyethyleneimine bead based on impact of sodium cation effect
URI https://dx.doi.org/10.1016/j.ijbiomac.2019.08.211
https://www.ncbi.nlm.nih.gov/pubmed/31465802
https://search.proquest.com/docview/2283115816
Volume 140
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