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Stabilizing biocatalysts
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Stereochemical Outcome of the Biocatalysed Reduction of Activated Tetrasubstituted Olefins by Old Yellow Enzymes 1–3
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Complementary Epoxide Hydrolase vs Glutathione S‐Transferase‐Catalyzed Kinetic Resolution of Simple Aliphatic Oxiranes–Complete Regio‐ and Enantioselective Hydrolysis of cis‐2‐Ethyl‐3‐methyloxirane
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Iterative Saturation Mutagenesis on the Basis of B Factors as a Strategy for Increasing Protein Thermostability
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Creation of an Amino Acid Network of Structurally Coupled Residues in the Directed Evolution of a Thermostable Enzyme
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Chitinase Inhibition by Chitobiose and Chitotriose Thiazolines
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Engineering Enzyme Stability and Resistance to an Organic Cosolvent by Modification of Residues in the Access Tunnel
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A. S. Bommarius and B. R. Riebel. Biocatalysis: fundamentals and applications. Wiley–VCH, 2004. 611 pp; ISBN 3‐527‐30344‐8
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Structure‐guided consensus approach to create a more thermostable penicillin G acylase
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Better library design: data‐driven protein engineering
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Biosynthetic concepts for the production of β‐lactam antibiotics in Penicillium chrysogenum
inferredcites →https://doi.org/10.1002/biot.201100486openalex-snapshot
Haloalkane dehalogenases: Biotechnological applications
inferredcites →https://doi.org/10.1002/bip.20800openalex-snapshot
Total synthesis by modern chemical ligation methods and high resolution (1.1 Å) X‐ray structure of ribonuclease A
inferredcites →https://doi.org/10.1002/bit.20107openalex-snapshot
Encapsulation of crosslinked penicillin G acylase aggregates in lentikats: Evaluation of a novel biocatalyst in organic media
inferredcites →https://doi.org/10.1002/bit.21292openalex-snapshot
The stability of engineered thermostable neutral proteases from Bacillus stearothermophilus in organic solvents and detergents
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Chimeric avidin shows stability against harsh chemical conditions—biochemical analysis and 3D structure
inferredcites →https://doi.org/10.1002/cbic.200700500openalex-snapshot
Development of a Thermostable Glucose Dehydrogenase by a Structure‐Guided Consensus Concept
inferredcites →https://doi.org/10.1002/cbic.200900570openalex-snapshot
Biocatalysis with Thermostable Enzymes: Structure and Properties of a Thermophilic ‘ene’‐Reductase related to Old Yellow Enzyme
inferredcites →https://doi.org/10.1002/cbic.201000213openalex-snapshot
The α/β‐Hydrolase Fold 3DM Database (ABHDB) as a Tool for Protein Engineering
inferredcites →https://doi.org/10.1002/cbic.201000464openalex-snapshot
Towards Practical Baeyer–Villiger‐Monooxygenases: Design of Cyclohexanone Monooxygenase Mutants with Enhanced Oxidative Stability
inferredcites →https://doi.org/10.1002/cbic.201100412openalex-snapshot
Enhancing the Thermal Robustness of an Enzyme by Directed Evolution: Least Favorable Starting Points and Inferior Mutants Can Map Superior Evolutionary Pathways
inferredcites →https://doi.org/10.1002/cbic.201200364openalex-snapshot
A pH‐Based High‐Throughput Assay for Transketolase: Fingerprinting of Substrate Tolerance and Quantitative Kinetics
inferredcites →https://doi.org/10.1002/cctc.200900120openalex-snapshot
Deactivation of TEM‐1 β‐Lactamase Investigated by Isothermal Batch and Non‐Isothermal Continuous Enzyme Membrane Reactor Methods
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Enhancing the Efficiency of Directed Evolution in Focused Enzyme Libraries by the Adaptive Substituent Reordering Algorithm
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Operational stability of Thermomyces lanuginosa lipase during interesterification of fat in continuous packed‐bed reactors
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Exploiting the Link between Protein Rigidity and Thermostability for Data‐Driven Protein Engineering
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Operational stability of cutinase in organic solvent system: model esterification of alkyl esters
inferredcites →https://doi.org/10.1002/pro.2031openalex-snapshot
Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: Factors contributing to increased activity retention
inferredcites →https://doi.org/10.1002/pro.281openalex-snapshot
The Hofmeister effect on amyloid formation using yeast prion protein
inferredcites →https://doi.org/10.1002/prot.20072openalex-snapshot
Topological thermal instability and length of proteins
inferredcites →https://doi.org/10.1002/prot.21227openalex-snapshot
Relative tolerance of mesostable and thermostable protein homologs to extensive mutation
inferredcites →https://doi.org/10.1006/jmbi.1994.1434openalex-snapshot
Sequence Statistics Reliably Predict Stabilizing Mutations in a Protein Domain
inferredcites →https://doi.org/10.1006/jmbi.1996.0633openalex-snapshot
Disallowed Ramachandran Conformations of Amino Acid Residues in Protein Structures
inferredcites →https://doi.org/10.1006/jmbi.2001.5043openalex-snapshot
Crystal structures of penicillin acylase enzyme-substrate complexes: structural insights into the catalytic mechanism 1 1Edited by K. Nagai
inferredcites →https://doi.org/10.1006/jmbi.2001.5152openalex-snapshot
The crystal structure of a hyper-thermophilic carboxylesterase from the archaeon Archaeoglobus fulgidus 1 1Edited by R. Huber
inferredcites →https://doi.org/10.1007/b96879openalex-snapshot
Immobilized Biocatalysts in Industrial Research and Production
inferredcites →https://doi.org/10.1007/bf01918191openalex-snapshot
Zur Lehre von der Wirkung der Salze
inferredcites →https://doi.org/10.1007/s00253-008-1412-7openalex-snapshot
Enhancing thermostability of Escherichia coli phytase AppA2 by error-prone PCR
inferredcites →https://doi.org/10.1007/s00253-011-3672-xopenalex-snapshot
Enzyme immobilization for biodiesel production
inferredcites →https://doi.org/10.1007/s00253-011-3817-yopenalex-snapshot
Efficient biocatalyst for large-scale synthesis of cephalosporins, obtained by combining immobilization and site-directed mutagenesis of penicillin acylase
inferredcites →https://doi.org/10.1007/s10822-007-9144-9openalex-snapshot
Rational design of an enzyme mutant for anti-cocaine therapeutics
inferredcites →https://doi.org/10.1007/s12257-012-0092-4openalex-snapshot
Stabilization of Candida antarctica lipase B in hydrophilic organic solvent by rational design of hydrogen bond
inferredcites →https://doi.org/10.1016/0003-9861(77)90434-9openalex-snapshot
Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
inferredcites →https://doi.org/10.1016/0141-0229(89)90084-7openalex-snapshot
Correlation between microbial protein thermostability and resistance to denaturation in aqueous: organic solvent two-phase systems
inferredcites →https://doi.org/10.1016/j.biochi.2012.05.013openalex-snapshot
Temperature adaptations in psychrophilic, mesophilic and thermophilic chloride-dependent alpha-amylases
inferredcites →https://doi.org/10.1016/j.bioeng.2004.12.003openalex-snapshot
Directed evolution of enzyme stability
inferredcites →https://doi.org/10.1016/j.biortech.2012.01.054openalex-snapshot
Biocatalyst development by directed evolution
inferredcites →https://doi.org/10.1016/j.biotechadv.2005.01.002openalex-snapshot
Structural features of thermozymes
inferredcites →https://doi.org/10.1016/j.biotechadv.2011.09.008openalex-snapshot
The imminent role of protein engineering in synthetic biology
inferredcites →https://doi.org/10.1016/j.bpc.2006.06.003openalex-snapshot
Stabilization of yeast hexokinase A by polyol osmolytes: Correlation with the physicochemical properties of aqueous solutions
inferredcites →https://doi.org/10.1016/j.cbpa.2007.05.006openalex-snapshot
Computational protein design: structure, function and combinatorial diversity
inferredcites →https://doi.org/10.1016/j.cbpa.2008.01.027openalex-snapshot
Advances in laboratory evolution of enzymes
inferredcites →https://doi.org/10.1016/j.cbpa.2010.11.011openalex-snapshot
Status of protein engineering for biocatalysts: how to design an industrially useful biocatalyst
inferredcites →https://doi.org/10.1016/j.ces.2009.12.005openalex-snapshot
Utilizing simple biochemical measurements to predict lifetime output of biocatalysts in continuous isothermal processes
inferredcites →https://doi.org/10.1016/j.chembiol.2006.08.006openalex-snapshot
Binding Properties of HABA-Type Azo Derivatives to Avidin and Avidin-Related Protein 4
inferredcites →https://doi.org/10.1016/j.copbio.2003.08.005openalex-snapshot
Metabolic engineering for the microbial production of 1,3-propanediol
inferredcites →https://doi.org/10.1016/j.copbio.2006.05.002openalex-snapshot
New opportunities revealed by biotechnological explorations of extremophiles
inferredcites →https://doi.org/10.1016/j.copbio.2010.08.011openalex-snapshot
Beyond directed evolution—semi-rational protein engineering and design
inferredcites →https://doi.org/10.1016/j.enzmictec.2006.04.024openalex-snapshot
Improved stabilization of microencapsulated Cathepsin B in harsh conditions
inferredcites →https://doi.org/10.1016/j.enzmictec.2010.10.003openalex-snapshot
Control of protein immobilization: Coupling immobilization and site-directed mutagenesis to improve biocatalyst or biosensor performance
inferredcites →https://doi.org/10.1016/j.enzmictec.2011.06.023openalex-snapshot
Enhancing the functional properties of thermophilic enzymes by chemical modification and immobilization
inferredcites →https://doi.org/10.1016/j.ijbiomac.2007.05.009openalex-snapshot
Mechanism of solvent induced thermal stabilization of papain
inferredcites →https://doi.org/10.1016/j.ijbiomac.2008.09.018openalex-snapshot
Co-solvent effects on structure and function properties of savinase: Solvent-induced thermal stabilization
inferredcites →https://doi.org/10.1016/j.jbiotec.2004.03.026openalex-snapshot
Rational engineering of enzyme stability
inferredcites →https://doi.org/10.1016/j.jbiotec.2011.07.016openalex-snapshot
The cellulose-binding domain of cellobiohydrolase Cel7A from Trichoderma reesei is also a thermostabilizing domain
inferredcites →https://doi.org/10.1016/j.jbiotec.2012.01.027openalex-snapshot
Thermostabilizing mutations preferentially occur at structural weak spots with a high mutation ratio
inferredcites →https://doi.org/10.1016/j.jbiotec.2012.02.014openalex-snapshot
Improved thermostability of AEH by combining B-FIT analysis and structure-guided consensus method
inferredcites →https://doi.org/10.1016/j.jmb.2005.10.011openalex-snapshot
Designing Thermostable Proteins: Ancestral Mutants of 3-Isopropylmalate Dehydrogenase Designed by using a Phylogenetic Tree
inferredcites →https://doi.org/10.1016/j.jmb.2008.04.024openalex-snapshot
Intense Neutral Drifts Yield Robust and Evolvable Consensus Proteins
inferredcites →https://doi.org/10.1016/j.jmb.2009.07.087openalex-snapshot
Structural Basis of Substrate Specificity of Plant 12-Oxophytodienoate Reductases
inferredcites →https://doi.org/10.1016/j.jmb.2009.08.008openalex-snapshot
Structural Redesign of Lipase B from Candida antarctica by Circular Permutation and Incremental Truncation
inferredcites →https://doi.org/10.1016/j.molcatb.2006.02.003openalex-snapshot
Development and characterization of recombinant whole-cell biocatalysts expressing epoxide hydrolase from Rhodotorula glutinis for enantioselective resolution of racemic epoxides
inferredcites →https://doi.org/10.1016/j.molcatb.2010.06.014openalex-snapshot
Amino ester hydrolase from Xanthomonas campestris pv. campestris, ATCC 33913 for enzymatic synthesis of ampicillin
inferredcites →https://doi.org/10.1016/j.molcatb.2011.04.013openalex-snapshot
NAD(P)H oxidase V from Lactobacillus plantarum (NoxV) displays enhanced operational stability even in absence of reducing agents
inferredcites →https://doi.org/10.1016/j.nbt.2010.08.012openalex-snapshot
Development and evaluation of data-driven designed tags (DDTs) for controlling protein solubility
inferredcites →https://doi.org/10.1016/j.procbio.2009.10.013openalex-snapshot
Promotion of multipoint covalent immobilization through different regions of genetically modified penicillin G acylase from E. coli
inferredcites →https://doi.org/10.1016/j.procbio.2012.07.023openalex-snapshot
A thermostable variant of P. aeruginosa cold-adapted LipC obtained by rational design and saturation mutagenesis
inferredcites →https://doi.org/10.1016/j.sbi.2010.06.001openalex-snapshot
Protein engineering for bioenergy and biomass-based chemicals
inferredcites →https://doi.org/10.1016/j.tetasy.2003.09.040openalex-snapshot
Highly enantioselective lipase-catalyzed reactions at high temperatures up to 120°C in organic solvent
inferredcites →https://doi.org/10.1016/j.tibtech.2009.08.001openalex-snapshot
Microbial biofilms: a concept for industrial catalysis?
inferredcites →https://doi.org/10.1016/j.ymeth.2004.03.021openalex-snapshot
Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process
inferredcites →https://doi.org/10.1016/s0006-3495(94)80711-8openalex-snapshot
Hofmeister effect in ion transport: reversible binding of halide anions to the roflamycoin channel
inferredcites →https://doi.org/10.1016/s0006-3495(97)78647-8openalex-snapshot
Charge density-dependent strength of hydration and biological structure
inferredcites →https://doi.org/10.1016/s0022-2836(03)00896-9openalex-snapshot
Designing Repeat Proteins: Well-expressed, Soluble and Stable Proteins from Combinatorial Libraries of Consensus Ankyrin Repeat Proteins
inferredcites →https://doi.org/10.1016/s0076-6879(04)88004-2openalex-snapshot
SCHEMA-Guided Protein Recombination
inferredcites →https://doi.org/10.1016/s0141-0229(00)00183-6openalex-snapshot
Prediction of penicillin V acylase stability in water-organic co-solvent monophasic systems as a function of solvent composition
inferredcites →https://doi.org/10.1016/s0167-4838(00)00238-7openalex-snapshot
The consensus concept for thermostability engineering of proteins
inferredcites →https://doi.org/10.1016/s0300-9629(97)00004-2openalex-snapshot
Thermophilic proteins: Stability and function in aqueous and organic solvents
inferredcites →https://doi.org/10.1016/s0958-1669(00)00229-9openalex-snapshot
Engineering proteins for thermostability: the use of sequence alignments versus rational design and directed evolution
inferredcites →https://doi.org/10.1016/s0959-440x(02)00347-0openalex-snapshot
Combinatorial protein design
inferredcites →https://doi.org/10.1016/s0968-0004(00)01755-2openalex-snapshot
How enzymes adapt: lessons from directed evolution
inferredcites →https://doi.org/10.1016/s0968-0004(01)01803-5openalex-snapshot
The temperature optima of enzymes: a new perspective on an old phenomenon
inferredcites →https://doi.org/10.1016/s0969-2126(98)00052-5openalex-snapshot
Structure of a microbial homologue of mammalian platelet-activating factor acetylhydrolases: Streptomyces exfoliatus lipase at 1.9 å resolution
inferredcites →https://doi.org/10.1016/s1367-5931(00)00182-4openalex-snapshot
Improved biocatalysts by directed evolution and rational protein design
inferredcites →https://doi.org/10.1016/s1381-1177(02)00075-9openalex-snapshot
Stabilization of horseradish peroxidase in aqueous-organic media by immobilization onto cellulose using a cellulose-binding-domain
inferredcites →https://doi.org/10.1017/s0033583500005369openalex-snapshot
The Hofmeister effect and the behaviour of water at interfaces
inferredcites →https://doi.org/10.1021/bi001139popenalex-snapshot
Crystal Structures of the Cellulase Cel48F in Complex with Inhibitors and Substrates Give Insights into Its Processive Action,
inferredcites →https://doi.org/10.1021/bi026131popenalex-snapshot
Biochemical Characterization and Structural Analysis of a Highly Proficient Cocaine Esterase,
inferredcites →https://doi.org/10.1021/bi201221jopenalex-snapshot
Second-Contact Shell Mutation Diminishes Streptavidin–Biotin Binding Affinity through Transmitted Effects on Equilibrium Dynamics
inferredcites →https://doi.org/10.1021/bi700844mopenalex-snapshot
Strain and Near Attack Conformers in Enzymic Thiamin Catalysis: X-ray Crystallographic Snapshots of Bacterial Transketolase in Covalent Complex with Donor Ketoses Xylulose 5-phosphate and Fructose 6-phosphate, and in Noncovalent Complex with Acceptor Aldose Ribose 5-phosphate
inferredcites →https://doi.org/10.1021/bi902052xopenalex-snapshot
Chiral Discrimination among Aminotransferases: Inactivation by 4-Amino-4,5-dihydrothiophenecarboxylic Acid
inferredcites →https://doi.org/10.1021/bm050947zopenalex-snapshot
Stabilization of a Formate Dehydrogenase by Covalent Immobilization on Highly Activated Glyoxyl-Agarose Supports
inferredcites →https://doi.org/10.1021/bp000023hopenalex-snapshot
Activation and Stabilization of Penicillin V Acylase from Streptomyces lavendulae in the Presence of Glycerol and Glycols
inferredcites →https://doi.org/10.1021/bp050249qopenalex-snapshot
Deactivation of Formate Dehydrogenase (FDH) in Solution and at Gas‐Liquid Interfaces
inferredcites →https://doi.org/10.1021/cm100823dopenalex-snapshot
Enzyme-Based Hybrid Macroporous Foams as Highly Efficient Biocatalysts Obtained through Integrative Chemistry
inferredcites →https://doi.org/10.1021/ja00299a044openalex-snapshot
Enzymatic vs. fermentative synthesis: thermostable glucose dehydrogenase catalyzed regeneration of NAD(P)H for use in enzymatic synthesis
inferredcites →https://doi.org/10.1021/ja01385a012openalex-snapshot
THE VISCOSITY OF AQUEOUS SOLUTIONS OF STRONG ELECTROLYTES WITH SPECIAL REFERENCE TO BARIUM CHLORIDE
inferredcites →https://doi.org/10.1021/ja066241+openalex-snapshot
Unexpected Acetylcholinesterase Activity of Cocaine Esterases
inferredcites →https://doi.org/10.1021/ja906212kopenalex-snapshot
Laboratory Evolution of Robust and Enantioselective Baeyer−Villiger Monooxygenases for Asymmetric Catalysis
inferredcites →https://doi.org/10.1021/ja970674iopenalex-snapshot
Substrate-Assisted Catalysis Unifies Two Families of Chitinolytic Enzymes
inferredcites →https://doi.org/10.1021/jo302484popenalex-snapshot
Chemoenzymatic Asymmetric Synthesis of Pregabalin Precursors via Asymmetric Bioreduction of β-Cyanoacrylate Esters Using Ene-Reductases
inferredcites →https://doi.org/10.1021/jp053618+openalex-snapshot
Evaluation of Hofmeister Effects on the Kinetic Stability of Proteins
inferredcites →https://doi.org/10.1021/jp7120164openalex-snapshot
Kinetic Model for Salt-Induced Protein Deactivation
inferredcites →https://doi.org/10.1021/la0528450openalex-snapshot
Increasing Protein Stability through Control of the Nanoscale Environment
inferredcites →https://doi.org/10.1021/op0600308openalex-snapshot
Chemocatalysis and Biocatalysis (Biotransformation): Some Thoughts of a Chemist and of a Biotechnologist
inferredcites →https://doi.org/10.1021/op7002248openalex-snapshot
Development of a Chemoenzymatic Manufacturing Process for Pregabalin
inferredcites →https://doi.org/10.1021/op900272dopenalex-snapshot
Development of a Biocatalytic Process as an Alternative to the (−)-DIP-Cl-Mediated Asymmetric Reduction of a Key Intermediate of Montelukast
inferredcites →https://doi.org/10.1021/sb300014topenalex-snapshot
SCHEMA-Designed Variants of Human Arginase I and II Reveal Sequence Elements Important to Stability and Catalysis
inferredcites →https://doi.org/10.1038/272581a0openalex-snapshot
Genes in pieces: were they ever together?
inferredcites →https://doi.org/10.1038/273267a0openalex-snapshot
Do genes-in-pieces imply proteins-in-pieces?
inferredcites →https://doi.org/10.1038/42990openalex-snapshot
Structure of isopenicillinN synthase complexed with substrate and the mechanism ofpenicillin formation
inferredcites →https://doi.org/10.1038/8213openalex-snapshot
Penicillin V acylase crystal structure reveals new Ntn-hydrolase family members.
inferredcites →https://doi.org/10.1038/nmeth1207-991openalex-snapshot
Protein engineers turned evolutionists
inferredcites →https://doi.org/10.1038/nprot.2007.321openalex-snapshot
The use of differential scanning fluorimetry to detect ligand interactions that promote protein stability
inferredcites →https://doi.org/10.1038/nrg2808openalex-snapshot
Mutational effects and the evolution of new protein functions
inferredcites →https://doi.org/10.1038/nsb742openalex-snapshot
Crystal structure of a bacterial cocaine esterase
inferredcites →https://doi.org/10.1039/b602579jopenalex-snapshot
Combining soft matter and soft chemistry: integrative chemistry towards designing novel and complex multiscale architectures
inferredcites →https://doi.org/10.1039/b814377copenalex-snapshot
High throughput methods of assessing protein stability and aggregation
inferredcites →https://doi.org/10.1039/b901172mopenalex-snapshot
Applications of biotransformations and biocatalysis to complexity generation in organic synthesis
inferredcites →https://doi.org/10.1039/b919115copenalex-snapshot
A green-by-design biocatalytic process for atorvastatin intermediate
inferredcites →https://doi.org/10.1039/c0cc02657copenalex-snapshot
Increasing the stability of an enzyme toward hostile organic solvents by directed evolution based on iterative saturation mutagenesis using the B-FIT method
inferredcites →https://doi.org/10.1039/c0ob00972eopenalex-snapshot
Computational design of a thermostable mutant of cocaine esterase via molecular dynamics simulations
inferredcites →https://doi.org/10.1039/c1cp21187kopenalex-snapshot
Protein stability in an ionic liquid milieu: on the use of differential scanning fluorimetry
inferredcites →https://doi.org/10.1039/c2cy20085fopenalex-snapshot
Biofilms and their engineered counterparts: A new generation of immobilised biocatalysts
inferredcites →https://doi.org/10.1039/c3cs35495dopenalex-snapshot
Conformational changes of enzymes upon immobilisation
inferredcites →https://doi.org/10.1039/c3cs60011dopenalex-snapshot
Whole-cell biocatalysis for selective and productive C–O functional group introduction and modification
inferredcites →https://doi.org/10.1042/bj1930285openalex-snapshot
The effects of surface and macromolecular interactions on the kinetics of inactivation of trypsin and α-chymotrypsin
inferredcites →https://doi.org/10.1042/bst0351558openalex-snapshot
Natural methods of protein stabilization: thermostable biocatalysts
inferredcites →https://doi.org/10.1042/bst0351602openalex-snapshot
Cation and strong co-solute effects on protein kinetic stability
inferredcites →https://doi.org/10.1046/j.1432-1033.2003.03923.xopenalex-snapshot
Mutational and computational analysis of the role of conserved residues in the active site of a family 18 chitinase
inferredcites →https://doi.org/10.1046/j.1432-1327.2000.01123.xopenalex-snapshot
Stabilization of NAD‐dependent formate dehydrogenase from Candida boidinii by site‐directed mutagenesis of cysteine residues
inferredcites →https://doi.org/10.1073/pnas.0510098103openalex-snapshot
Protein stability promotes evolvability
inferredcites →https://doi.org/10.1073/pnas.0901417106openalex-snapshot
A family of thermostable fungal cellulases created by structure-guided recombination
inferredcites →https://doi.org/10.1073/pnas.0901522106openalex-snapshot
In the light of directed evolution: Pathways of adaptive protein evolution
inferredcites →https://doi.org/10.1073/pnas.170145497openalex-snapshot
Novel folded protein domains generated by combinatorial shuffling of polypeptide segments
inferredcites →https://doi.org/10.1073/pnas.84.5.1219openalex-snapshot
Designing substrate specificity by protein engineering of electrostatic interactions.
inferredcites →https://doi.org/10.1073/pnas.90.11.5076openalex-snapshot
Three-dimensional structures of avidin and the avidin-biotin complex.
inferredcites →https://doi.org/10.1073/pnas.92.12.5553openalex-snapshot
Sticky ions in biological systems.
inferredcites →https://doi.org/10.1073/pnas.94.16.8411openalex-snapshot
Three-dimensional structure of NADPH–cytochrome P450 reductase: Prototype for FMN- and FAD-containing enzymes
inferredcites →https://doi.org/10.1073/pnas.96.6.2591openalex-snapshot
A hierarchical approach to protein molecular evolution
inferredcites →https://doi.org/10.1074/jbc.275.18.13708openalex-snapshot
Directed Evolution of β-Glucosidase A from Paenibacillus polymyxa to Thermal Resistance
inferredcites →https://doi.org/10.1074/jbc.c109.034058openalex-snapshot
SCHEMA Recombination of a Fungal Cellulase Uncovers a Single Mutation That Contributes Markedly to Stability
inferredcites →https://doi.org/10.1074/jbc.m300815200openalex-snapshot
Why Is Trehalose an Exceptional Protein Stabilizer?
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The Sequence and Crystal Structure of the α-Amino Acid Ester Hydrolase from Xanthomonas citri Define a New Family of β-Lactam Antibiotic Acylases
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inferred← citeshttps://doi.org/10.1016/b978-0-12-409547-2.14571-8openalex-snapshot
Enzymatic Reactions and Biocatalytic Processes
inferred← citeshttps://doi.org/10.1016/b978-0-12-411518-7.00004-4openalex-snapshot
Enzyme Immobilization for Organic Synthesis
inferred← citeshttps://doi.org/10.1016/b978-0-12-800217-9.00005-8openalex-snapshot
Chemical stabilization of enzymes
inferred← citeshttps://doi.org/10.1016/b978-0-12-800217-9.00009-5openalex-snapshot
Selected industrial enzymes
inferred← citeshttps://doi.org/10.1016/b978-0-12-803725-6.00007-8openalex-snapshot
Metagenomics and the Search for Industrial Enzymes
inferred← citeshttps://doi.org/10.1016/b978-0-12-803725-6.00015-7openalex-snapshot
Microbial Enzymes for Glycoside Synthesis
inferred← citeshttps://doi.org/10.1016/b978-0-12-816984-1.00024-xopenalex-snapshot
Metal-organic frameworks (MOFs) for enzyme immobilization
inferred← citeshttps://doi.org/10.1016/b978-0-12-819539-0.00005-1openalex-snapshot
Biocatalysis in green organic synthesis
inferred← citeshttps://doi.org/10.1016/b978-0-12-822887-6.00019-xopenalex-snapshot
Industrial production of enzymes for use in animal-feed bioprocessing
inferred← citeshttps://doi.org/10.1016/b978-0-12-824436-4.00007-1openalex-snapshot
Enzyme immobilized nanomaterials
inferred← citeshttps://doi.org/10.1016/b978-0-12-824436-4.00016-2openalex-snapshot
Therapeutic applications
inferred← citeshttps://doi.org/10.1016/b978-0-32-390644-9.00123-2openalex-snapshot
Flow Biocatalysis for Chiral Molecules Synthesis
inferred← citeshttps://doi.org/10.1016/b978-0-323-91317-1.00004-9openalex-snapshot
Selection and modification of enzymes prior to immobilization
inferred← citeshttps://doi.org/10.1016/b978-0-323-95251-4.00016-8openalex-snapshot
Bacterial enzymes and their application in agroecology
inferred← citeshttps://doi.org/10.1016/b978-0-323-98386-0.00013-0openalex-snapshot
Applications of high-hydrostatic-pressure processing on microbial enzymes
inferred← citeshttps://doi.org/10.1016/b978-0-443-15562-8.00007-8openalex-snapshot
Artificial enzymes in homogeneous catalysis
inferred← citeshttps://doi.org/10.1016/b978-0-443-18810-7.00003-xopenalex-snapshot
Enzyme-like activity of nanozymes, the enzyme mimics
inferred← citeshttps://doi.org/10.1016/b978-0-443-23998-4.00011-7openalex-snapshot
Whole-cell biocatalysis for large-scale production
inferred← citeshttps://doi.org/10.1016/bs.apha.2022.06.001openalex-snapshot
Use of engineered cytochromes P450 for accelerating drug discovery and development
inferred← citeshttps://doi.org/10.1016/bs.mie.2018.03.005openalex-snapshot
Haloalkane Dehalogenases From Marine Organisms
inferred← citeshttps://doi.org/10.1016/bs.mie.2020.09.008openalex-snapshot
Optimizing the linker length for fusing an alcohol dehydrogenase with a cyclohexanone monooxygenase
inferred← citeshttps://doi.org/10.1016/bs.mie.2025.01.080openalex-snapshot
Biocatalysis: Important considerations for testing and evaluation of biocatalysts
inferred← citeshttps://doi.org/10.1016/j.ab.2022.114796openalex-snapshot
Comparing the effects of organic cosolvents on acetylcholinesterase and butyrylcholinesterase activity
inferred← citeshttps://doi.org/10.1016/j.abb.2017.11.006openalex-snapshot
Kinetics and thermodynamics of the thermal inactivation and chaperone assisted folding of zebrafish dihydrofolate reductase
inferred← citeshttps://doi.org/10.1016/j.abb.2024.110246openalex-snapshot
Tools to investigate oxygen-related challenges with flavin-dependent enzymes
inferred← citeshttps://doi.org/10.1016/j.aca.2026.345864openalex-snapshot
Driven magnetic 3D DNA walker coupled with CHA based on light-activatable hairpin: A dual-amplification strategy for ultrasensitive hantavirus RNA sensing
inferred← citeshttps://doi.org/10.1016/j.apcata.2018.08.003openalex-snapshot
Controlled manipulation of enzyme specificity through immobilization-induced flexibility constraints
inferred← citeshttps://doi.org/10.1016/j.bbagen.2017.10.008openalex-snapshot
Identification, characterization, immobilization, and mutational analysis of a novel acetylesterase with industrial potential ( La AcE) from Lactobacillus acidophilus
inferred← citeshttps://doi.org/10.1016/j.bbrep.2020.100856openalex-snapshot
A versatile tool in controlling aggregation and Ag nanoparticles assisted in vitro folding of thermally denatured zDHFR
inferred← citeshttps://doi.org/10.1016/j.bcab.2019.101038openalex-snapshot
Surface functionalization of SBA-15 for immobilization of lipase and its application in synthesis of alkyl levulinates: Optimization and kinetics
inferred← citeshttps://doi.org/10.1016/j.bcab.2019.101064openalex-snapshot
Amino acid induced hyper activation of laccase and its application in dye degradation
inferred← citeshttps://doi.org/10.1016/j.bej.2024.109260openalex-snapshot
A paradigm shift for biocatalytic microreactors: Decoupling application from reactor design
inferred← citeshttps://doi.org/10.1016/j.bej.2025.110050openalex-snapshot
Leveraging histidine-nickel coordination for stable enzyme immobilization on metal-organic frameworks
inferred← citeshttps://doi.org/10.1016/j.biortech.2022.127886openalex-snapshot
Directed reconstruction of a novel ancestral alcohol dehydrogenase featuring shifted pH-profile, enhanced thermostability and expanded substrate spectrum
inferred← citeshttps://doi.org/10.1016/j.biortech.2025.132769openalex-snapshot
Synergistic low-temperature petroleum remediation via surfactant-modified biochar and cold-tolerant microorganisms
inferred← citeshttps://doi.org/10.1016/j.biortech.2026.134103openalex-snapshot
Site-directed mutagenesis to enhance thermostability of Caulobacter sp. D5 ω-transaminase for efficient bioamination of biobased aldehydes
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2018.10.011openalex-snapshot
The state-of-the-art strategies of protein engineering for enzyme stabilization
inferred← citeshttps://doi.org/10.1016/j.biotechadv.2025.108607openalex-snapshot
Innovations in smart enzyme biosensors: Advancing the detection of antibiotic residues in aquaculture
inferred← citeshttps://doi.org/10.1016/j.biteb.2026.103126openalex-snapshot
Revolutionizing leather processing: Enzymatic dehairing for a sustainable future
inferred← citeshttps://doi.org/10.1016/j.cattod.2015.05.004openalex-snapshot
Advanced characterization of immobilized enzymes as heterogeneous biocatalysts
inferred← citeshttps://doi.org/10.1016/j.cattod.2015.05.027openalex-snapshot
Chemical amination of lipases improves their immobilization on octyl-glyoxyl agarose beads
inferred← citeshttps://doi.org/10.1016/j.cbpa.2013.12.003openalex-snapshot
Computational tools for designing and engineering enzymes
inferred← citeshttps://doi.org/10.1016/j.cej.2024.151580openalex-snapshot
Tannic acid mediated hollow biocatalytic zeolitic imidazolate frameworks as a “three-in-one” label for enhancing the sensitivity of fluorescence immunosensor
inferred← citeshttps://doi.org/10.1016/j.cej.2024.154375openalex-snapshot
Unlocking opportunities: Supported metal catalysts for the chemical upcycling of waste plastics
inferred← citeshttps://doi.org/10.1016/j.cels.2020.08.016openalex-snapshot
Fast and Flexible Protein Design Using Deep Graph Neural Networks
inferred← citeshttps://doi.org/10.1016/j.ces.2019.04.020openalex-snapshot
Enhancing the thermostability of β-glucuronidase from T. pinophilus enables the biotransformation of glycyrrhizin at elevated temperature
inferred← citeshttps://doi.org/10.1016/j.checat.2022.09.036openalex-snapshot
Modern computational methods for rational enzyme engineering
inferred← citeshttps://doi.org/10.1016/j.cherd.2021.11.026openalex-snapshot
α-Glucosidase enzyme entrapped superporous poly(amphoteric) cryogel reactor with improved enzymatic activity and stability over wide pH ranges
inferred← citeshttps://doi.org/10.1016/j.chroma.2026.467062openalex-snapshot
Quantification of residual protein from biocatalysts employed in the synthesis of pharmaceutical drug substances using reversed-phase HPLC
inferred← citeshttps://doi.org/10.1016/j.cis.2025.103589openalex-snapshot
Enzyme immobilization based on reticular framework materials: Strategy, food applications, and prospect
inferred← citeshttps://doi.org/10.1016/j.cis.2026.103996openalex-snapshot
Orchestrating molecular threads into functional networks: Supramolecular hydrogels as dynamic scaffolds for enzyme immobilization and catalysis
inferred← citeshttps://doi.org/10.1016/j.cogsc.2023.100787openalex-snapshot
Developments on oxidase stability
inferred← citeshttps://doi.org/10.1016/j.colsurfa.2025.136973openalex-snapshot
Modulating the activity and stability of Cyt c in a covalent organic framework by regulating the covalent interactions
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2019.02.018openalex-snapshot
Site-specific, covalent immobilization of an engineered enterokinase onto magnetic nanoparticles through transglutaminase-catalyzed bioconjugation
inferred← citeshttps://doi.org/10.1016/j.colsurfb.2020.111052openalex-snapshot
Biological metal organic framework (bio-MOF) of glucoamylase with enhanced stability
inferred← citeshttps://doi.org/10.1016/j.compchemeng.2017.01.015openalex-snapshot
Bioprocess intensification for the effective production of chemical products
inferred← citeshttps://doi.org/10.1016/j.compchemeng.2018.05.014openalex-snapshot
Computational design of thermostable mutants for cephalosporin C acylase from Pseudomonas strain SE83
inferred← citeshttps://doi.org/10.1016/j.compositesb.2021.108788openalex-snapshot
Improved enzymatic activity by oriented immobilization on graphene oxide with tunable surface heterogeneity
inferred← citeshttps://doi.org/10.1016/j.copbio.2023.103058openalex-snapshot
Cell-free chemoenzymatic cascades with bio-based molecules
inferred← citeshttps://doi.org/10.1016/j.csbj.2020.12.034openalex-snapshot
Can constraint network analysis guide the identification phase of KnowVolution? A case study on improved thermostability of an endo-β-glucanase
inferred← citeshttps://doi.org/10.1016/j.csbj.2022.05.008openalex-snapshot
Protposer: The web server that readily proposes protein stabilizing mutations with high PPV
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2016.10.011openalex-snapshot
Deciphering the factors defining the pH-dependence of a commercial glycoside hydrolase family 8 enzyme
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2019.109413openalex-snapshot
Semi-rational engineering of a Kluyveromyces lactis aldo-keto reductase KlAKR for improved catalytic efficiency towards t-butyl 6-cyano-(3R, 5R)-dihydroxyhexanoate
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2022.110040openalex-snapshot
Modification to increase the thermostability and catalytic efficiency of α-L-rhamnosidase from Bacteroides thetaiotaomicron and high-level expression
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2022.110052openalex-snapshot
Thermostabilizing ketoreductase ChKRED20 by consensus mutagenesis at dimeric interfaces
inferred← citeshttps://doi.org/10.1016/j.enzmictec.2024.110517openalex-snapshot
Changes in ficin specificity by different substrate proteins promoted by enzyme immobilization
inferred← citeshttps://doi.org/10.1016/j.fbio.2023.103119openalex-snapshot
Improving the thermostability of glycosyltransferase UGT76G1 by computer-aided target analysis for highly efficient biosynthesis of rebaudioside M
inferred← citeshttps://doi.org/10.1016/j.fbp.2023.03.007openalex-snapshot
Food processing applications of protease activity identified in the methotrexate degrading enzyme of Variovorax paradoxus
inferred← citeshttps://doi.org/10.1016/j.febslet.2014.11.033openalex-snapshot
Structural and biochemical characterization of a carbohydrate acetylesterase from Sinorhizobium meliloti 1021
inferred← citeshttps://doi.org/10.1016/j.heliyon.2024.e32435openalex-snapshot
Enzymatic synthesis of pyridine heterocyclic compounds and their thermal stability
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2016.12.061openalex-snapshot
Characterization of a novel SGNH-type esterase from Lactobacillus plantarum
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.02.092openalex-snapshot
Combi-metal organic framework (Combi-MOF) of α-amylase and glucoamylase for one pot starch hydrolysis
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.08.126openalex-snapshot
Magnetic-metal organic framework (magnetic-MOF): A novel platform for enzyme immobilization and nanozyme applications
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2018.09.078openalex-snapshot
Improving the retention and reusability of Alpha-amylase by immobilization in nanoporous polyacrylamide-graphene oxide nanocomposites
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.01.240openalex-snapshot
Enzyme embedded metal organic framework (enzyme–MOF): De novo approaches for immobilization
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.11.053openalex-snapshot
Stability and refolding of Dihydrofolate reductase enhances with nano-conjugation
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2020.12.068openalex-snapshot
Structure-based mechanisms: On the way to apply alcohol dehydrogenases/reductases to organic-aqueous systems
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.05.167openalex-snapshot
Stabilization of immobilized lipases by treatment with metallic phosphate salts
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2022.12.074openalex-snapshot
Designing multifunctional biocatalytic cascade system by multi-enzyme co-immobilization on biopolymers and nanostructured materials
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.123968openalex-snapshot
Magnetic metal-organic frameworks immobilized enzyme-based nano-biocatalytic systems for sustainable biotechnology
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.125447openalex-snapshot
Enhancing the thermostability of carboxypeptidase A by a multiple computer-aided rational design based on amino acids preferences at β-turns
inferred← citeshttps://doi.org/10.1016/j.ijbiomac.2023.125853openalex-snapshot
Glutaraldehyde modification of lipases immobilized on octyl agarose beads: Roles of the support enzyme loading and chemical amination of the enzyme on the final enzyme features
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