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Varavinit, Saiyavit; Chaokasem, Narisa; Shobsngob, Sujin

doi:10.1023/a:1012984802624

Cited by 45 publications

(8 citation statements)

References 10 publications

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“…While these residual activities are a low percentage of the original activity, they are comparable to reported values for cellulose-immobilized enzymes. 29 …”

Section: Resultsmentioning

confidence: 99%

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

et al. 2004

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A new method for introducing enzymes into cellulosic matrixes which can be formed into membranes, films, or beads has been developed using a cellulose-in-ionic-liquid dissolution and regeneration process. Initial results on the formation of thin cellulose films incorporating dispersed laccase indicate that active enzyme-encapsulated films can be prepared using this methodology and that precoating the enzyme with a second, hydrophobic ionic liquid prior to dispersion in the cellulose/ionic liquid solution can provide an increase in enzyme activity relative to that of untreated films, presumably by providing a stabilizing microenvironment for the enzyme.

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“…While these residual activities are a low percentage of the original activity, they are comparable to reported values for cellulose-immobilized enzymes. 29 …”

Section: Resultsmentioning

confidence: 99%

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

et al. 2004

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“…In the light of these considerations, it is possible to propose that covalent binding provides the strongest attachment of the enzyme to the support, and it has been associated with high activities and the possibility of enzyme reuses. However, covalent attachment is generally achieved using complex chemicals as linkers, in multi-step reactions that require relatively long times to be completed [113]. Aiming to circumvent these disadvantages, Hirsh et al [108] obtained a highly effective method for rapid covalent immobilization (within one minute reaction) using plasma immersion ion implantation (PIII) for activation of polystyrene film polymer surface.…”

Section: The Gh1 Family Of Enzymesmentioning

confidence: 99%

Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives

et al. 2016

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Glycoside hydrolases (GH) are enzymes capable to hydrolyze the glycosidic bond between two carbohydrates or even between a carbohydrate and a non-carbohydrate moiety. Because of the increasing interest for industrial applications of these enzymes, the immobilization of GH has become an important development in order to improve its activity, stability, as well as the possibility of its reuse in batch reactions and in continuous processes. In this review, we focus on the broad aspects of immobilization of enzymes from the specific GH families. A brief introduction on methods of enzyme immobilization is presented, discussing some advantages and drawbacks of this technology. We then review the state of the art of enzyme immobilization of families GH1, GH13, and GH70, with special attention on the enzymes β-glucosidase, α-amylase, cyclodextrin glycosyltransferase, and dextransucrase. In each case, the immobilization protocols are evaluated considering their positive and negative aspects. Finally, the perspectives on new immobilization methods are briefly presented.

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“…18 It has a large potential to be used in many applications due to its biodegradable and biocompatible. 19 Bacterial cellulose has the same molecular formula as plant cellulose, it can be modied by periodate oxidation to give rise to a C2, 3-dialdehyde BC for potential biodegradable tissue engineering scaffolds. 20 Aer modication of BC into C2, 3-dialdehyde BC, tensile strength and Young's modulus drop down distinctly.…”

Section: Introductionmentioning

confidence: 99%