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Enzyme–Polymer Conjugates to Enhance Enzyme Shelf Life in a Liquid Detergent Formulation
Author(s) -
Kübelbeck Sonja,
Mikhael Jules,
Keller Harald,
Konradi Rupert,
AndrieuBrunsen Annette,
Baier Grit
Publication year - 2018
Publication title -
macromolecular bioscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.924
H-Index - 105
eISSN - 1616-5195
pISSN - 1616-5187
DOI - 10.1002/mabi.201800095
Subject(s) - chemistry , reductive amination , candida antarctica , lipase , polymer , immobilized enzyme , aldehyde , conjugated system , enzyme , organic chemistry , covalent bond , conjugate , maltodextrin , combinatorial chemistry , chromatography , spray drying , catalysis , mathematical analysis , mathematics
Abstract 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.