Hexanal and t-2-hexenal form covalent bonds with whey proteins and sodium caseinate in aqueous solution

2004 ◽  
Vol 14 (8) ◽  
pp. 681-690 ◽  
Author(s):  
Anne Meynier ◽  
Vincent Rampon ◽  
Michèle Dalgalarrondo ◽  
Claude Genot
Keyword(s):  
Aqueous Solution ◽  
Whey Proteins ◽  
Sodium Caseinate ◽  
Covalent Bonds

scholarly journals Application of free and immobilized laccase for removal and detoxification of fluoroquinolones from aqueous solution

2020 ◽  
Keyword(s):  
Aqueous Solution ◽  
Trametes Versicolor ◽  
Storage Stability ◽  
Hydroxybenzoic Acid ◽  
Bacterial Strains ◽  
Covalent Bonds ◽  
Immobilized Laccase ◽  
And Storage

<p>Laccase from Trametes versicolor was immobilized by covalent bonds formation on CPC silica carriers. Elimination of two floroqinolone (FQ); enrofloxacine (ENR) and flumequine (FLU) using laccase in both free and immobilized form in the absence and presence of 1-hydroxybenzotriazole (HBT) and 4-Hydroxybenzoic acid (HBA) as mediators was investigated. Temperature, pH and storage stability of immobilized laccase was significantly improved compare to free laccase. In the absence of a laccase mediator, the initial concentrations of 50 mg L–1 of ENR and FLU decreased by 19 % and 28 %, respectively, after 6 h treatment using the immobilized laccase, while, the removal percentages were increased to 98 % and 96 %, respectively, when the immobilized laccase was used in presence of HBT. Whereas, the removal percentages of ENR and FLU were increased to 97 % and 88 %, respectively, when the immobilized laccase was used in presence of HBA. After twenty runs of the enzymatic elimination (laccase-HBT system) of ENR and FLU, the immobilized laccase exhibited the relative removal of 17.63 % and 15.62 %, respectively. The results of microtoxicity test (growth inhabitation percentage of six bacterial strains) showed a significant decrease in toxicity of the laccase-treated ENR and FLU solution.</p>

scholarly journals Influence of enzymatic cow milk hydrolysates on IgA and IgG response of Balb/c mice organism

2011 ◽  
Vol 23 (No. 2) ◽  
pp. 51-63 ◽  
Author(s):  
B. Wróblewska ◽  
L. Jędrychowski
Keyword(s):  
Whey Proteins ◽  
Sodium Caseinate ◽  
Cow Milk ◽  
Whey Protein Concentrate ◽  
Protein Concentrate ◽  
Peptide Fraction ◽  
Beneficial Impact ◽  
Molecular Masses ◽  
Specific Igg ◽  
Hydrolysis Of

The manuscript presents the application of an animal model, Balb/c mice, in studies aimed at identifying among enzymatic hydrolysates of sodium caseinate and whey proteins the product with the most beneficial impact on the animal organism. One- and two-step hydrolyses were carried out using the following enzymes: Alcalase (Novo Nordisk), papain (Sigma), and Lactozym (Novo Nordisk). Estimations were also made with a peptide fraction, the so-called II fraction, of WPC (Whey Protein Concentrate) and Alcalase hydrolysate with molecular masses lower than 12.4 kDa. The levels of specific IgG and IgA were determined in blood serum and intestinal extracts of mice. The hydrolysis of sodium caseinate with the use of Alcalase was found to affect the reduction in the material allergenicity. Of all whey hydrolysates, the most promising results were obtained upon the application of the II fraction of WPC and Alcalase hydrolysate (M.W. &lt; 12.4 kDa). &nbsp; &nbsp;

Effect of phospholipid molecular structure on its interaction with whey proteins in aqueous solution

2013 ◽  
Vol 32 (2) ◽  
pp. 312-321 ◽  
Author(s):  
M. Kasinos ◽  
P. Sabatino ◽  
B. Vanloo ◽  
K. Gevaert ◽  
J.C. Martins ◽  
...  
Keyword(s):  
Molecular Structure ◽  
Aqueous Solution ◽  
Whey Proteins

Reversible cold gelation of sodium caseinate solutions with added salt

2004 ◽  
Vol 71 (1) ◽  
pp. 126-128 ◽  
Author(s):  
Alistair J Carr ◽  
Peter A Munro
Keyword(s):  
Viscosity Solutions ◽  
Calcium Ions ◽  
Apparent Viscosity ◽  
Whey Proteins ◽  
Sodium Caseinate ◽  
High Viscosity ◽  
Divalent Salts ◽  
Added Salt

During a study on the effect of addition of monovalent and divalent salts on the apparent viscosity of sodium caseinate solutions (Carr et al. 2002) it was discovered that many of the high viscosity solutions appeared to gel when refrigerated. Furthermore this cold gelation was found to reverse on heating. The phenomenon of reversible cold gelation of caseinate solutions has not been reported. The most well known example of reversible cold gelation is gelatin solutions, but a number of polysaccharides also form gels on cooling, e.g. agarose, pectin and carrageenan (Evans & Wennerstrom, 1994). Whey proteins also gel at 25 °C in the presence of calcium ions, though not in their absence, and this gelation is not reversible (Barbut & Foegeding, 1993).

Investigations of the Effects of Salt and Biopolymer Ratio on Sodium Caseinate-Xanthan Interactions in Aqueous Solution and Emulsions

2014 ◽  
Vol 35 (3) ◽  
pp. 390-396 ◽  
Author(s):  
Nadji Moulai-Mostefa ◽  
Nadjia Sabri ◽  
Razika Khalladi ◽  
Abdelkader HadjSadok
Keyword(s):  
Aqueous Solution ◽  
Sodium Caseinate

Heat-induced aggregation of whey proteins in the presence of κ-casein or sodium caseinate

2009 ◽  
Vol 23 (4) ◽  
pp. 1103-1110 ◽  
Author(s):  
Fanny Guyomarc'h ◽  
Merveille Nono ◽  
Taco Nicolai ◽  
Dominique Durand
Keyword(s):  
Whey Proteins ◽  
Sodium Caseinate ◽  
Induced Aggregation

Effect of sucrose on molecular and interaction parameters of sodium caseinate in aqueous solution: relationship to protein gelation

2003 ◽  
Vol 31 (1-4) ◽  
pp. 31-46 ◽  
Author(s):  
Larisa E Belyakova ◽  
Anna S Antipova ◽  
Maria G Semenova ◽  
Eric Dickinson ◽  
Lara Matia Merino ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Sodium Caseinate ◽  
Interaction Parameters ◽  
Protein Gelation

A transient non-covalent hydrogel by a supramolecular gelator with dynamic covalent bonds

2021 ◽  
Vol 45 (10) ◽  
pp. 4773-4779
Author(s):  
Sahabaj Mondal ◽  
Debasish Haldar
Keyword(s):  
Aqueous Solution ◽  
Self Assembly ◽  
Covalent Bonds ◽  
Solution Equilibrium ◽  
Low Concentration ◽  
Non Equilibrium

In aqueous solution, equilibrium self-assembly and gelation occur at higher concentration but on addition of EDC non-equilibrium self-assembly and transient hydrogels are formed at low concentration, which dissolve upon anhydride hydrolysis.

Production of Protein-Coated Low-Fat Potato Chips

2005 ◽  
Vol 11 (3) ◽  
pp. 177-181 ◽  
Author(s):  
M. Aminlari ◽  
R. Ramezani ◽  
M. H. Khalili
Keyword(s):  
Storage Time ◽  
Corn Oil ◽  
Whey Proteins ◽  
Sodium Caseinate ◽  
Egg White ◽  
Potato Chips ◽  
Oil Uptake ◽  
Sodium Bisulphite ◽  
Egg White Proteins ◽  
Potato Slices

The purpose of this study was to prepare protein-coated potato chips and evaluate type of proteins and storage time on the quality of final product. Potato slices were prepared, blanched, immersed in solutions of sodium caseinate, whey proteins concentrate (WPC), or egg white and deep-fried in a mixture of corn oil and commercial hydrogenated oil. Chips were packed and stored for different times. The results showed that sodium bisulphite in blanching solution improved binding of proteins to potato slices. Protein coating resulted in significantly lower oil uptake of potato chips. Coating potato chips with sodium caseinate, WPC and egg white proteins resulted in 14, 5 and 12% reduction in oil uptake, respectively. Water retention and protein content significantly increased in protein-coated chips. Peroxide values increased with storage time in all samples. Protein-coated chips had a decrease in peroxide value between 30 to 50%. Sensory evaluation of chips showed that at all storage time intervals, flavour of sodium caseinate-coated chips were more acceptable than non-coated, WPC or egg white protein-coated chips.

Sign in / Sign up

Export Citation Format

Share Document