A5042832154- Proteins in Food Systems
- Microencapsulation and Drying Processes
- Microbial Inactivation Methods
- Meat and Animal Product Quality
- Magnetic and Electromagnetic Effects
- Enzyme Production and Characterization
- Listeria monocytogenes in Food Safety
- Protein Hydrolysis and Bioactive Peptides
- Food Allergy and Anaphylaxis Research
- Food Chemistry and Fat Analysis
- Freezing and Crystallization Processes
- Food Industry and Aquatic Biology
- Escherichia coli research studies
- Phytase and its Applications
- Food composition and properties
- Probiotics and Fermented Foods
- nanoparticles nucleation surface interactions
- Muscle metabolism and nutrition
- Pickering emulsions and particle stabilization
- Botanical Research and Applications
- Polysaccharides Composition and Applications
- Biomedical Research and Pathophysiology
- Advanced Drug Delivery Systems
- Ocular Surface and Contact Lens
- Electromagnetic Launch and Propulsion Technology
Université de Montpellier
2009-2021
Ingénierie des Agropolymères et Technologies Emergentes
2008-2021
Centre de Biologie Structurale
1992-2003
University of California, Davis
1998
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTHigh-Pressure Unfolding and Aggregation of .beta.-Lactoglobulin the Baroprotective Effects SucroseEliane M. Dumay, Monica T. Kalichevsky, J. Claude CheftelCite this: Agric. Food Chem. 1994, 42, 9, 1861–1868Publication Date (Print):September 1, 1994Publication History Published online1 May 2002Published inissue 1 September 1994https://pubs.acs.org/doi/10.1021/jf00045a006https://doi.org/10.1021/jf00045a006research-articleACS PublicationsRequest reuse...
Solutions of β-lactoglobulin (β-Lg) isolate (23 g protein/kg, pH 7.0, in 50 mM Bis-Tris buffer) were either flushed with N2 or O2 brought to given concentrations N-ethylmaleimide (NEM), β-mercaptoethanol (MSH), cysteine (CYS), glutathione (GSH) and then pressurized at 450 MPa 25 °C for 5, 15, 30 min. Sulfhydryl groups (SH), half-cystine residues, S−S bonds not influenced by pressure (0−30 min), without prior flushing N2, thus revealing no significant oxidation SH groups. Polyacrylamide gel...
Ovalbumin solutions (2%, pH 7.0, 200 ohm·cm) and dialyzed fresh egg white (pH 9.2, 200−250 were subjected to 50−400 exponential decay pulses with an electric field strength of 27−33 kV/cm. The pulse width was ca. 0.3 μs (at a capacitance 20 nF) or 0.9 80 nF), the corresponding dissipated energy 0.7 2.3 J/(pulse·mL) solution. sample temperature maintained below 29 °C. While four sulfhydryl groups native ovalbumin did not react DTNB, they became reactive immediately after processing,...
The phase diagram of water as a function temperature and pressure delimits distinct crystalline ice forms with different specific volumes, melting temperatures, latent heats fusion. I decreases to −22°C when increases 207.5 MPa. It is possible freeze biological or food sample under (obtaining I, III, V, VI, VII), enhance nucleation by fast release, keep at subzero temperatures without crystal formation, generate through freezing, reach the glassy state cooling pressure, thaw frozen below...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSurface hydrophobicity and aggregation of .beta.-lactoglobulin heated near neutral pHAnne Laligant, Eliane Dumay, Carmen Casas Valencia, Jean Louis Cuq, Claude CheftelCite this: J. Agric. Food Chem. 1991, 39, 12, 2147–2155Publication Date (Print):December 1, 1991Publication History Published online1 May 2002Published inissue 1 December 1991https://pubs.acs.org/doi/10.1021/jf00012a009https://doi.org/10.1021/jf00012a009research-articleACS...
Solutions of a β-lactoglobulin isolate in water, potassium phosphate buffer (20 or 50 mmol/L), and pressure-resistant buffers, at protein concentration 25 g/kg pH 7.0, were processed 150, 250, 350 450 MPa °C, for 15 min, then stored 4 usually 24 h, before analysis. Bis-Tris mmol/L) bis-Tris-propane (10, 20 selected as while the water is known to decrease reversibly by 0.2–0.3 unit per 100 MPa. After pressurization, nitrogen solubility 4.7 aggregation patterns polyacrylamide gel...
Raw whole milk of high microbial quality ([les ]4×10 4 cfu/ml) was processed using a ~15 l/h homogeniser with pressure (HP) valve immediately followed by cooling heat exchangers. The effects homogenisation between 100 and 300 MPa (HP valve) an initial temperature T in =4 °C or 24 investigated on the inactivation of: (i) endogenous alkaline phosphatase (ALP); (ii) flora (iii) two Gram positive ( Listeria innocua Micrococcus luteus ) one negative Pseudomonas fluorescens strains inoculated into...
ABSTRACT A whey protein isolate (WPI) was coagulated by thermomechanical processing in a twin screw extruder. Nonaggregated semi‐solid spreads were obtained only the pH range 3.5–3.9, at ca 20% (77% water), barrel temperature of 90–100°C and speed 100–200 rpm. WPI extrusion‐coagulated 3.9 displayed high nitrogen solubility (NSI) (43–47%). Electrophoresis indicated that β‐lactoglobulin constituent entirely soluble 1% SDS, while scanning calorimetry revealed about 82% unfolding. 4.5–6.8 lower...