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Enzyme–Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation

Herein, the synthesis of enzyme–polymer conjugates is reported. Four different activated polymers (mPEG‐aldehyde, mPEG‐NHS, maltodextrin‐aldehyde, carboxymethyl cellulose aldehyde) are conjugated to the surface of protease, α‐amylase, and lipase using two different strategies (reductive amination an...

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Published in:Macromolecular bioscience 2018-07, Vol.18 (7), p.e1800095-n/a
Main Authors: Kübelbeck, Sonja, Mikhael, Jules, Keller, Harald, Konradi, Rupert, Andrieu‐Brunsen, Annette, Baier, Grit
Format: Article
Language:English
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Summary:Herein, the synthesis of enzyme–polymer conjugates is reported. Four different activated polymers (mPEG‐aldehyde, mPEG‐NHS, maltodextrin‐aldehyde, carboxymethyl cellulose aldehyde) are conjugated to the surface of protease, α‐amylase, and lipase using two different strategies (reductive amination and alkylation with NHS‐activated acid). Although the chemical modification of the enzymes is accompanied by losses in enzyme activity (maximum loss 40%), the covalent attachment of polymers increases the thermal stability and the stability in a standard detergent formulation compared to the unmodified enzymes. The enzyme–polymer conjugates are characterized by asymmetrical‐flow field‐flow fractionation and differential scanning microcalorimetry. Furthermore, it is demonstrated that conjugated enzymes still show performance in a real washing process. Enzyme–polymer conjugates show a potential as a stabilizing system for enzymes in detergents. The synthesis of enzyme–polymer conjugates is reported. Four different activated polymers are conjugated to the surface of three enzymes using two different strategies. Although the chemical modification of the enzymes is accompanied by slight losses in enzyme activity, the covalent attachment of polymers increases the thermal stability and the stability in a standard detergent formulation compared to the unmodified enzymes.
ISSN:1616-5187
1616-5195
DOI:10.1002/mabi.201800095