Reference health

Enzyme immobilization on smart polymers: Catalysis on demand

https://doi.org/10.1016/j.reactfunctpolym.2014.07.010
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1 of 46 checkable references need attention · checked 2026-07-22

At the dated check, the references listed below either did not resolve in Crossref or DataCite, or carried a retraction notice. Each one is shown with the registry record that put it there.

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References needing attention

marked retracted — notice via Crossref, record curated by Retraction Watch10.1016/j.biortech.2012.09.012
RETRACTED: Role and significance of beta-glucosidases in the hydrolysis of cellulose for bioethanol production
The 45 checked references that resolve
resolves10.1038/nrm3274
Understanding the language of Lys36 methylation at histone H3
resolves10.1258/ebm.2011.011152
The antioxidant enzyme peroxiredoxin and its protective role in neurological disorders
resolves10.1007/s00018-012-0988-3
γ-Glutamyltranspeptidases: sequence, structure, biochemical properties, and biotechnological applications
resolves10.1111/1574-6968.12057
Industrial waste based compost as a source of novel cellulolytic strains and enzymes
resolves10.1016/j.jbiotec.2012.06.037
Glucansucrases: Three-dimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications
resolves10.1016/j.biotechadv.2011.10.007
Biocatalytic ketone reduction: A green and efficient access to enantiopure alcohols
resolves10.1007/s00253-012-4312-9
Features and applications of bilirubin oxidases
resolves10.3390/ijms14011232
From Protein Engineering to Immobilization: Promising Strategies for the Upgrade of Industrial Enzymes
resolves10.1016/j.biortech.2011.11.054
Immobilization of biocatalysts for enzymatic polymerizations: Possibilities, advantages, applications
resolves10.1016/j.biotechadv.2011.09.005
Potential applications of enzymes immobilized on/in nano materials: A review
resolves10.1021/ja307308j
Gold Nanoparticles as Electronic Bridges for Laccase-Based Biocathodes
resolves10.1016/j.jcis.2011.07.095
Immbolization of uricase enzyme in Langmuir and Langmuir-Blodgett films of fatty acids: Possible use as a uric acid sensor
resolves10.1016/j.jcis.2010.05.041
Synthesis of colloidal silica nanoparticles of a tunable mesopore size and their application to the adsorption of biomolecules
resolves10.1007/s12154-013-0102-9
Enzyme immobilization: an update
resolves10.1039/C3CS60075K
Enzyme immobilisation in biocatalysis: why, what and how
resolves10.1039/c3cs35511j
Evaluation of immobilized enzymes for industrial applications
resolves10.1016/j.biortech.2011.08.011
Integrating photobiological hydrogen production with dye–metal bioremoval from simulated textile wastewater
resolves10.1007/s00253-011-3094-9
Covalent immobilization of recombinant Rhizobium etli CFN42 xylitol dehydrogenase onto modified silica nanoparticles
resolves10.1039/c3cs35506c
Industrial use of immobilized enzymes
resolves10.1039/C1SM06452E
Multi-enzyme systems: bringing enzymes together in vitro
resolves10.1016/j.biotechadv.2011.09.003
Immobilization strategies to develop enzymatic biosensors
resolves10.1039/c3tb20116c
Immobilization of trypsin via reactive polymer grafting from magnetic nanoparticles for microwave-assisted digestion
resolves10.1016/0013-4686(94)E0054-4
Conducting polymer-based biosensors
resolves10.1021/la001164w
Pepsin−Gold Colloid Conjugates:  Preparation, Characterization, and Enzymatic Activity
resolves10.1021/nl025778s
Alumina−Pepsin Hybrid Nanoparticles with Orientation-Specific Enzyme Coupling
resolves10.1016/j.biosystems.2004.03.001
Use of chemically modified PMMA microspheres for enzyme immobilization
resolves10.1021/ac1023099
Coupling Formic Acid Assisted Solubilization and Online Immobilized Pepsin Digestion with Strong Cation Exchange and Microflow Reversed-Phase Liquid Chromatography with Electrospray Ionization Tandem Mass Spectrometry for Integral Membrane Proteome Analysis
resolves10.1021/ac301749h
Pepsin Immobilized on High-Strength Hybrid Particles for Continuous Flow Online Digestion at 10 000 psi
resolves10.1016/j.chroma.2008.02.075
In-line system containing porous polymer monoliths for protein digestion with immobilized pepsin, peptide preconcentration and nano-liquid chromatography separation coupled to electrospray ionization mass spectroscopy
resolves10.1016/j.aca.2008.04.060
Pepsin immobilized in dextran-modified fused-silica capillaries for on-line protein digestion and peptide mapping
resolves10.1007/s10404-012-1031-6
Non-denaturing low-temperature bonding of patterned poly(methyl methacrylate) enzymatic microreactors
resolves10.1007/s12633-009-9002-6
Immobilization and Activity of Pepsin in Silicone Elastomers
resolves10.1021/bm400762h
Heterofunctional Supports in Enzyme Immobilization: From Traditional Immobilization Protocols to Opportunities in Tuning Enzyme Properties
resolves10.1208/s12249-010-9429-5
Negative Thermo-responsive Microspheres Based on Hydrolyzed Gelatin as Drug Delivery Device
resolves10.1016/j.reactfunctpolym.2010.07.017
Synthesis, characterization and application of poly(N-isopropylacrylamide-co-itaconic acid) hydrogels as supports for lipase immobilization
resolves10.1016/S0168-3659(99)00176-5
Glutaraldehyde crosslinked sodium alginate beads containing liquid pesticide for soil application
resolves10.1016/j.foodchem.2013.06.046
Is it possible to screen for milk or whey protein adulteration with melamine, urea and ammonium sulphate, combining Kjeldahl and classical spectrophotometric methods?
resolves10.1002/biot.200500022
Properties of immobilized pepsin on Modified PMMA microspheres
resolves10.1016/j.ijpharm.2013.02.023
Incorporation of carbon nanotubes into a gelatin–catechin conjugate: Innovative approach for the preparation of anticancer materials
resolves10.1016/j.ejpb.2010.05.008
Grafted thermo-responsive gelatin microspheres as delivery systems in triggered drug release
resolves10.1007/s11051-013-1581-x
Biodegradable gelatin-based nanospheres as pH-responsive drug delivery systems
resolves10.1016/j.freeradbiomed.2005.09.039
Sensitizer-mediated photooxidation of histidine residues: Evidence for the formation of reactive side-chain peroxides
resolves10.1016/S1011-1344(01)00208-1
Photo-oxidation of proteins and its role in cataractogenesis
resolves10.1016/j.carbpol.2013.10.022
Influence of polymer network parameters of tragacanth gum-based pH responsive hydrogels on drug delivery
resolves10.1016/j.foodchem.2005.11.005
Immobilization of pepsin on chitosan beads
The 4 references without a DOI — listed, not checked
no DOI — not checked10.1016/j.reactfunctpolym.2014.07.010_b0015
no DOI — not checked10.1016/j.reactfunctpolym.2014.07.010_b0095
no DOI — not checked10.1016/j.reactfunctpolym.2014.07.010_b0240
no DOI — not checked10.1016/j.reactfunctpolym.2014.07.010_b0250
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