2013
DOI: 10.1002/asia.201300850
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Biocatalytic Performance of pH‐Sensitive Magnetic Nanoparticles Derived from Layer‐by‐Layer Ionic Self‐Assembly of Chitosan with Glucoamylase

Abstract: Based on the characteristics of polycations of chitosan and glucoamylase, which are oppositely charged, they were successfully alternatingly deposited onto the surface of aldehyde-modified Fe3O4 nanoparticles by using a layer-by-layer ion exchange method to form magnetic carriers to construct multilayer films (designated as Fe3O4@(CS/GA)n). The (CS/GA)n film systems were endowed with the pH-dependent properties of chitosan as well as the catalytic activity of glucoamylase. The changes in weight loss and surfac… Show more

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Cited by 5 publications
(4 citation statements)
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“…GA is an enzyme capable of hydrolyzing starch into glucose ( 32 ). The negatively stained high-resolution transmission electron microscope (HRTEM) image reveals that GA/Pt is highly monodispersed, and the Pt nanoparticle is inside GA.…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…GA is an enzyme capable of hydrolyzing starch into glucose ( 32 ). The negatively stained high-resolution transmission electron microscope (HRTEM) image reveals that GA/Pt is highly monodispersed, and the Pt nanoparticle is inside GA.…”
Section: Resultsmentioning
confidence: 99%
“…We further used PE-GA/Pt 2 for hydrogel photopatterning. In a three-enzyme cascade reaction, PE-GA/Pt 2 catalyzes the hydrolysis of starch into glucose ( 32 ), and then, glucose oxidase (GOx) catalyzes the oxidation of glucose to hydrogen peroxide (H 2 O 2 ) (Fig. 3A) ( 35 ).…”
Section: Resultsmentioning
confidence: 99%
“…Therefore, such magnetic/CS microspheres with perfect monodispersity would be an ideal support for enzyme immobilization [93]. In a further study, Wang et al [94] obtained an alternative layered assembly of CS and glucoamylase on the surface of aldehyde modified Fe 3 O 4 MNPs via ion exchange method. Five layer immobilized glucoamylase had excellent catalytic activity, storage and pH stability, and reusability as compared to soluble enzyme.…”
Section: α-Amylasementioning
confidence: 99%
“…Glucoamylases immobilized on/ in nanosupports retained remarkably high stability against the inactivation mediated by pH, heat, inhibitors, products, and storage as compared to soluble enzyme. Such immobilized enzyme preparations were found highly stable on prolonged use in the reactors and on repeated uses in batch processes [92][93][94][95][96].…”
Section: α-Amylasementioning
confidence: 99%