Repository hosted by TU Delft Library

Home · Contact · About · Disclaimer ·
 

Search results also available in MS Excel format.

Showing 1 to 10 of 10 found. | Sort by date

1 Sample geometry as critical factor for stability research
article 2003    
Author: Klerk, W.P.C. de · Boers, M.N.
Keywords: Filling degree · Grinding · Heat flow · Microcalorimetry · Propellants · Stability · gunpowder · oxygen · propellant · conference paper · decomposition · humidity · measurement · microcalorimetry · surface property · thermostability · Oxygen, 7782-44-7
[Abstract]

2 Deglycosylation of ovalbumin prohibits formation of a heat-stable conformer
article 2007    
Author: Groot, J.de · Kosters, H.A. · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Circular dichroism · Deglycosylation · Ovalbumin · PNGase-F · S-ovalbumin · Size exclusion chromatography · Thermostability · Carbohydrate moiety · Deglycosylation · Ovalbumin · Thermostability · Carbohydrates · Differential scanning calorimetry · Heat treatment · pH effects · Reaction kinetics · Size exclusion chromatography · Thermodynamic stability · Proteins · glycopeptidase · ovalbumin · s ovalbumin · unclassified drug · article · circular dichroism · deglycosylation · differential scanning calorimetry · enzyme binding · gel permeation chromatography · mass spectrometry · protein conformation · protein denaturation · thermostability · Animals · Chickens · Chromatography, Gel · Circular Dichroism · Enzyme Stability · Glycosylation · Heat · Isoelectric Focusing · Mass Spectrometry · Molecular Weight · Ovalbumin · Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase · Protein Conformation · Spectrometry, Fluorescence
[Abstract]

3 Glycoforms of β-Lactoglobulin with Improved Thermostability and Preserved Structural Packing
article 2004    
Author: Broersen, K. · Voragen, A.G.J. · Hamer, R.J. · Jongh, H.H.J. de
Keywords: Nutrition · Food technology · β-Lactoglobulin · Glycosylation · Maillard reaction · Monosaccharides · Thermal stability · Amines · Glucose · Hydrophobicity · Proteins · Thermodynamics · Structural stability · Thermostability · Biotechnology · beta lactoglobulin · amino acid sequence · analytic method · article · chemical modification · hydrophobicity · normal distribution · protein secondary structure · protein structure · protein tertiary structure · structure analysis · thermostability · Fructose · Glucose · Glycosylation · Hydrogen-Ion Concentration · Lactoglobulins · Macromolecular Substances · Protein Binding · Protein Conformation · Protein Denaturation · Protein Isoforms · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Receptors, Fc · Temperature
[Abstract]

4 Purification, cloning and characterisation of two forms of thermostable and highly active cellobiohydrolase I (Cel7A) produced by the industrial strain of Chrysosporium lucknowense
article 2005    
Author: Gusakov, A.V. · Sinitsyn, A.P. · Salanovich, T.N. · Bukhtojarov, F.E. · Markov, A.V. · Ustinov, B.B. · Zeijl, C.V. · Punt, P. · Burlingame, R.
Keywords: Biology · Biotechnology · Cellobiohydrolase · Cellulase · Chrysosporium lucknowense · Purification · Trichoderma reesei · Adsorption · Cellulose · Data acquisition · Differential scanning calorimetry · Fungi · Hydrolysis · Mass spectrometry · Cellobiohydrolase I (CBH I, CeI7A) · Cellulases · Chrysosporium lucknowense · Thermostability · Enzymes · cellulose 1,4 beta cellobiosidase · adsorption · amino acid sequence · article · catalysis · Chrysosporium · Chrysosporium lucknowense · controlled study · differential scanning calorimetry · enzyme activity · glycosylation · high temperature · hydrolysis · matrix assisted laser desorption ionization time of flight mass spectrometry · molecular cloning · molecular dynamics · nonhuman · nucleotide sequence · purification · thermostability · Adsorption · Calorimetry · Cellulose · Data Processing · Enzymes · Fungi · Hydrolysis · Chrysosporium · Chrysosporium lucknowense · Fungi · Gossypium hirsutum · Hypocrea jecorina · Trichoderma
[Abstract]

5 The presence of heat-stable conformers of ovalbumin affects properties of thermally formed aggregates
article 2003    
Author: Groot, J.de · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Aggregation · Ovalbumin · Protein denaturation · Stokes radius · Turbidity · ovalbumin · article · chemical reaction kinetics · heat treatment · pH · priority journal · protein aggregation · protein analysis · protein denaturation · protein stability · thermostability · turbidity · Animals · Calorimetry, Differential Scanning · Chickens · Heat · Kinetics · Ovalbumin · Protein Conformation · Time Factors · Gallus gallus
[Abstract]

6 HNF/HTPB propellants: Influence of HNF particle size on ballistic properties
article 2009    
Author: Heijden, A.E.D.M. van der · Leeuwenburgh, A.B.
Keywords: Ballistics · Ballistic properties · Oxidizer size · Propellants · Ballistic properties · Burning rate · Coarse particles · Grinding process · Hydrazinium nitroformate · Hydroxyl-terminated polybutadiene · Mean size · Oxidizer size · Pressure exponents · Propellant burning rate · Solid composites · Thermal stability · Ballistics · Butadiene · Explosives · Particle size · Propellants · Stability · Spacecraft propulsion · 1,3 butadiene derivative · hydrazine derivative · article · combustion · controlled study · grinding · particle size · priority journal · thermostability
[Abstract]

7 Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties
article 1999    
Author: Koppelman, S.J. · Bruijnzeel-Koomen, C.A.F.M. · Hessing, M. · Jongh, H.H.J. de
Keywords: Allergen · Allergenicity · Animal cell · Conformational transition · Heat tolerance · Isoelectric point · Nonhuman · Peanut · Priority journal · Protein denaturation · Protein family · Protein folding · Protein secondary structure · Solubility · Thermostability · Adult · Allergens · Arachis hypogaea · Calorimetry, Differential Scanning · Chromatography, Gel · Circular Dichroism · Glycoproteins · Heat · Humans · Immunoglobulin E · Plant Proteins · Protein Conformation · Spectrophotometry, Ultraviolet · Animalia · Ara · Arachis hypogaea
[PDF] [Abstract]

8 Chemical processing as a tool to generate ovalbumin variants with changed stability
article 2003    
Author: Kosters, H.A. · Broersen, K. · Groot, J.de · Simons, J.W.F.A. · Wierenga, P. · Jongh, H.H.J.de
Keywords: Nutrition · Food technology · Chemical processing · Modification · Ovalbumin · Structural integrity · Thermostability · Chemical modification · Differential scanning calorimetry · Fluorescence · Proteins · Thermodynamics · Chemical processing · Biotechnology · guanidine · ovalbumin · tryptophan · alkalinity · article · chemical procedures · covalent bond · denaturation · energy · lipophilicity · methylation · protein binding · protein folding · protein modification · protein processing · protein stability · spectroscopy · temperature dependence · thermodynamics · Animals · Chemical Industry · Chickens · Drug Stability · Hydrogen-Ion Concentration · Hydrophobicity · Ovalbumin · Protein Conformation · Protein Denaturation · Protein Folding · Protein Structure, Quaternary · Protein Structure, Secondary · Protein Structure, Tertiary · Temperature
[Abstract]

9 Heat-induced conformational changes of patatin, the major potato tuber protein
article 1998    
Author: Pots, A.M. · Jongh, H.H.J. de · Gruppen, H. · Hamer, R.J. · Voragen, A.G.J.
Keywords: Nutrition · Conformational change · Patatin · Solanum tuberosum · Enzyme · Vegetable protein · Alpha helix · Circular dichroism · Conformational transition · Differential scanning calorimetry · Enzyme conformation · Enzyme inactivation · Fluorescence spectroscopy · Infrared spectroscopy · Nonhuman · Potato · Priority journal · Protein denaturation · Protein folding · Protein secondary structure · Temperature · Thermostability · Butyrates · Calorimetry, Differential Scanning · Carboxylic Ester Hydrolases · Circular Dichroism · Enzyme Stability · Esterases · Plant Proteins · Protein Conformation · Protein Folding · Protein Structure, Secondary · Protein Structure, Tertiary · Solanum tuberosum · Spectrometry, Fluorescence · Spectroscopy, Fourier Transform Infrared · Temperature · Tryptophan · Solanum tuberosum · Tuberosum
[Abstract]

10 Amylomaltase of Pyrobaculum aerophilum IM2 produces thermoreversible starch gels
article 2005    
Author: Kaper, T. · Talik, B. · Ettema, T.J. · Bos, H. · Maarel, M.J.E.C. van der · Dijkhuizen, L.
Keywords: Nutrition · Food technology · Escherichia coli · Gels · Glucose · Mathematical models · pH effects · Starch · Achaeal amylomaltase · Amylomaltase · Binding mode · Pyrobaculum aerophilum IM2 · Enzyme kinetics · 4alpha glucanotransferase · acarbose · cysteine · disulfide · dithiothreitol · gelatin · gene product · glucan · glucose · glycosidase · hydroxyl group · oligosaccharide · potato starch · starch · enzyme · Archean · article · chemical reaction kinetics · enzyme active site · enzyme activity · enzyme inhibition · enzyme substrate complex · Escherichia coli · food industry · gene expression · heat sensitivity · molecular cloning · nonhuman · Pyrobaculum · pyrobaculum aerophilum · thermostability · Binding Sites · Cloning, Molecular · Enzyme Stability · Escherichia coli · Food Industry · Gels · Glycogen Debranching Enzyme System · Heat · Kinetics · Pyrobaculum · Starch · Archaea · Escherichia coli · Pyrobaculum aerophilum · Solanum tuberosum
[PDF] [Abstract]

Search results also available in MS Excel format.

Showing 1 to 10 of 10 found. | Sort by date