2022
DOI: 10.1080/10242422.2022.2082871
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A biocatalytic system obtained via immobilization of urease onto magnetic metal/alginate nanocomposite: Improving reusability and enhancing stability

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Cited by 5 publications
(2 citation statements)
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“…The successful immobilization of the β-glucosidase may have resulted from permanent crosslinking of the enzyme and carrier by EDC/NHS, as suggested by immobilization of the enzyme via strong covalent binding to CS-MIL-Fe. The enzyme efficacy was improved as the steric barriers surrounding the enzyme active sites were reduced due to the large surface area of the carrier and dispersion of the enzyme [ 33 , 34 ]. The robust chemical linkages between MOFs and enzymes are thought to involve covalent bonds [ 35 ].…”
Section: Resultsmentioning
confidence: 99%
“…The successful immobilization of the β-glucosidase may have resulted from permanent crosslinking of the enzyme and carrier by EDC/NHS, as suggested by immobilization of the enzyme via strong covalent binding to CS-MIL-Fe. The enzyme efficacy was improved as the steric barriers surrounding the enzyme active sites were reduced due to the large surface area of the carrier and dispersion of the enzyme [ 33 , 34 ]. The robust chemical linkages between MOFs and enzymes are thought to involve covalent bonds [ 35 ].…”
Section: Resultsmentioning
confidence: 99%
“…This immobilization efficiency at pH 6 is related to the ionizable groups of the enzyme which has more cationic groups at pH 6 than at pH 7 because its isoelectric point is 8.7 [ 26 ]. Changes in the ionic character of the enzyme surface can impact its interaction with the support surface, altering adsorption properties, orientation, or localized ionic repulsion/attraction [ 27 ].
Figure 1 Schematic representation for the synthesis of PET-hydrazide/GO and enzyme immobilization.
…”
Section: Resultsmentioning
confidence: 99%