Functional Stabilization of Cellulase from <i>Aspergillus niger</i> by Conjugation with Dextran-aldehyde

Arslan, Aslı; Kuzu, Huriye; Altıkatoğlu, Melda

doi:10.1080/07328303.2010.508140

Cited by 6 publications

(7 citation statements)

References 34 publications

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“…By far, the most employed strategy to prepare neoglycoenzymes is the covalent cross-linking with periodate-oxidized oligo- and polysaccharide via reductive alkylation (Figure ). ,− ,,,,− Meta periodate ion cleaves C–C bonds that possess adjacent hydroxyl groups by oxidation to highly reactive aldehydes. This approach permits one to control the oxidation level of the carbohydrate by manipulating the m -NaIO 4 /monosaccharide ratio .…”

Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

Neoglycoenzymes

et al. 2014

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Section: Strategies For Preparing Artificial Glycoenzymesmentioning

confidence: 99%

Neoglycoenzymes

et al. 2014

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“…Dextran (3 in Figure 2), a highly hydrophilic neutral polysaccharide, which is also used as the support of enzymes. A cellulase conjugate of cellulase and dextran was prepared by Arslan et al [45]. The cellulase/dextran conjugate showed better activity and thermal stability than the free enzyme [45].…”

Section: Natural Polymersmentioning

confidence: 99%

Immobilization of Enzymes by Polymeric Materials

et al. 2021

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Enzymes are the highly efficient biocatalyst in modern biotechnological industries. Due to the fragile property exposed to the external stimulus, the application of enzymes is highly limited. The immobilized enzyme by polymer has become a research hotspot to empower enzymes with more extraordinary properties and broader usage. Compared with free enzyme, polymer immobilized enzymes improve thermal and operational stability in harsh environments, such as extreme pH, temperature and concentration. Furthermore, good reusability is also highly expected. The first part of this study reviews the three primary immobilization methods: physical adsorption, covalent binding and entrapment, with their advantages and drawbacks. The second part of this paper includes some polymer applications and their derivatives in the immobilization of enzymes.

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“…Although dexOx is a random coil molecule with scarce rigidity, some authors tried to increase the enzyme rigidity using intramolecular covalent crosslinking. For instance, soluble cellulase from Aspergillus niger was modified using dexOx, with a significant improvement in enzyme stability versus inactivation, both thermal or mediated by sodium dodecylsulfate [144]. In another example, dextran sulfate was oxidized with periodate, and this polysaccharide was employed to modify an α-amylase from Aspergillus oryzae, maintaining the enzymatic activity at a pH value lower than that the one for the non-modified enzyme [145].…”

Section: Glycosylation Of Enzymes and Promotion Of Intramolecular Cromentioning

confidence: 99%

“…Thus D-amino acid oxidase, glucose oxidase and trypsin were coated with dexOx, reporting and increase in stability of the immobilized enzymes in the presence of hydrophobic interfaces [171]. In another paper, cellulase from Aspergillus niger modified with dexOx was described to be more stable in the presence of air bubbles (residual activity of about 50% for 4 h) [144]; correspondingly, horseradish peroxidase modified with dexOx was not only more stable and active than the free enzyme in presence of an organic-aqueous interface, but also became less prone to suffer inhibition in the presence of heavy metal salts and various denaturing compounds [172]. This stabilization versus interaction with hydrophobic interfaces was later extrapolated to the enzymes immobilized on nonporous nanoparticles (Figure 8).…”

Section: Glycosylation Of Enzymes and Promotion Of Intramolecular Cromentioning

confidence: 99%

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

et al. 2019

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Dextran aldehyde (dexOx), resulting from the periodate oxidative cleavage of 1,2-diol moiety inside dextran, is a polymer that is very useful in many areas, including as a macromolecular carrier for drug delivery and other biomedical applications. In particular, it has been widely used for chemical engineering of enzymes, with the aim of designing better biocatalysts that possess improved catalytic properties, making them more stable and/or active for different catalytic reactions. This polymer possesses a very flexible hydrophilic structure, which becomes inert after chemical reduction; therefore, dexOx comes to be highly versatile in a biocatalyst design. This paper presents an overview of the multiple applications of dexOx in applied biocatalysis, e.g., to modulate the adsorption of biomolecules on carrier surfaces in affinity chromatography and biosensors design, to serve as a spacer arm between a ligand and the support in biomacromolecule immobilization procedures or to generate artificial microenvironments around the enzyme molecules or to stabilize multimeric enzymes by intersubunit crosslinking, among many other applications.

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Functional Stabilization of Cellulase from Aspergillus niger by Conjugation with Dextran-aldehyde

Cited by 6 publications

References 34 publications

Neoglycoenzymes

Neoglycoenzymes

Immobilization of Enzymes by Polymeric Materials

Dextran Aldehyde in Biocatalysis: More Than a Mere Immobilization System

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