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1.
J Agric Food Chem ; 62(10): 2284-8, 2014 Mar 12.
Article in English | MEDLINE | ID: mdl-24559153

ABSTRACT

Scanning electrochemical microscopy (SECM) combined with a Langmuir trough was used for studying oxygen transfer across protein films at an air-water interface. The method allows the comparison of the oxygen permeability of different emulsifiers without any concerns of interference of atmospheric oxygen. Two milk proteins, ß-lactoglobulin and ß-casein, were compared, and the permeabilities obtained were for ß-casein PD ≈ 2.2 × 10(-7) cm(2)/s and for ß-lactoglobulin PD ≈ 0.6 × 10(-7) cm(2)/s, which correspond to the lowest limit of the diffusion coefficients and are 2 orders of magnitude lower than the diffusion coefficient of oxygen in water, yet several orders of magnitude higher than previously reported for milk protein films. The method allows characterization of the oxygen barrier properties of liquid interfacial films, which is of crucial importance for understanding the role of the interface in the inhibition of oxygen transport and developing modified interfaces with higher oxygen blocking efficacy.


Subject(s)
Milk Proteins/chemistry , Oxygen/chemistry , Air , Caseins/chemistry , Lactoglobulins/chemistry , Microscopy, Electrochemical, Scanning , Models, Chemical , Permeability , Water/chemistry
2.
Food Chem ; 144: 50-6, 2014 Feb 01.
Article in English | MEDLINE | ID: mdl-24099541

ABSTRACT

Distribution of protein and oil in aqueous and spray-dried emulsions and the effect of protein cross-linking on emulsion properties and matrix-water interactions were investigated. Sodium caseinate and sunflower oil were used to make emulsions which were spray dried using maltodextrin as a wall material. 3% Na-caseinate concentration showed optimum emulsion and process stability as observed in CLSM images, droplet size data and in the amount of heptane-extractable oil from spray-dried emulsions. Transglutaminase cross-linking prior to emulsification slightly increased the amount of protein both on the oil droplet interface and on the particle surface as confirmed by analysis of continuous phase protein in the feed emulsion and by XPS measurements from the powder surface. DSC and water sorption measurements were used to study the physical state of the matrix. Glass transition occurred between RH 54% and 75% at room temperature and it was not affected by cross-linking.


Subject(s)
Caseins/chemistry , Emulsions/chemistry , Animals , Cattle , Desiccation , Food Technology , Particle Size , Powders
3.
Food Chem ; 144: 57-64, 2014 Feb 01.
Article in English | MEDLINE | ID: mdl-24099542

ABSTRACT

The aim of this work was to investigate how the oxidative stability of encapsulated oil is affected by the humidity response of a Na-caseinate-maltodextrin matrix. Furthermore, the effect of modification of the interfacial Na-caseinate layer through cross-linking was studied. For this purpose, two model spray-dried emulsions containing sunflower oil, maltodextrin, and either non-cross-linked or cross-linked Na-caseinate were stored at different relative humidities (RHs; ∼0%, 11%, 33%, 54%, and 75%). Increasing RH improved the oxidative stability of the spray-dried emulsions. This behaviour was mainly linked to the loss of individual powder particles upon caking and collapsing of the matrix at RH 75%. Oxidation of non-encapsulated surface lipids with a proportion of ca. 5% of total lipids was only twofold compared to total lipids. Excess protein on particle surfaces may have delayed oxidation, e.g., by its radical scavenging activity. Under several storage conditions, cross-linking of the protein slightly improved the oxidative stability.


Subject(s)
Caseins/chemistry , Emulsions/chemistry , Desiccation , Food Technology , Oxidation-Reduction , Plant Oils/chemistry , Polysaccharides/chemistry , Powders/chemistry , Sunflower Oil
4.
J Agric Food Chem ; 60(24): 6223-9, 2012 Jun 20.
Article in English | MEDLINE | ID: mdl-22655797

ABSTRACT

Sodium caseinate was modified by transglutaminase catalyzed cross-linking reaction prior to the emulsification process in order to study the effect of cross-linking on the oxidative stability of protein stabilized emulsions. The extent of the cross-linking catalyzed by different dosages of transglutaminase was investigated by following the ammonia production during the reaction and using SDS-PAGE gel. O/W emulsions prepared with the cross-linked and non-cross-linked sodium caseinates were stored for 30 days under the same conditions. Peroxide value measurement, oxygen consumption measurement, and headspace gas chromatography analysis were used to study the oxidative stability of the emulsions. The emulsion made of the cross-linked sodium caseinate showed an improved oxidative stability with reduced formation of fatty acid hydroperoxides and volatiles and a longer period of low rate oxygen consumption. The improving effect of transglutaminase catalyzed cross-linking could be most likely attributed to the enhanced physical stability of the interfacial protein layer against competitive adsorption by oil oxidation products.


Subject(s)
Caseins/metabolism , Cross-Linking Reagents/metabolism , Emulsions/chemistry , Linseed Oil/chemistry , Transglutaminases/metabolism , Ammonia/metabolism , Drug Stability , Electrophoresis, Polyacrylamide Gel , Lipid Peroxides/metabolism , Oxidation-Reduction , Oxygen/metabolism
5.
J Agric Food Chem ; 59(24): 13246-53, 2011 Dec 28.
Article in English | MEDLINE | ID: mdl-22060038

ABSTRACT

Whey protein isolate was modified by ethylene diamine in order to shift its isoelectric point to an alkaline pH. The extent of the modification was studied using SDS-PAGE and MALDI-TOF mass spectrometry. The modified whey proteins were used as an emulsifier to stabilize oil-in-water emulsions at acidic and neutral pH ranges, and their emulsifying properties were compared with that of the unmodified whey proteins and with the previously studied ethylene diamine modified sodium caseinate. The emulsifying activity of the modified whey proteins was similar to that of the unmodified ones, but the stability of an emulsion at pH 5 was significantly improved after the modification. Charge and coverage of droplet surface and the displacement of the interfacial proteins by surfactant Tween 20 were further studied as a function of pH. As compared with the unmodified whey proteins, the modified ones were proven to cover the interface more efficiently with extensive surface charge at pH 5, although the interfacial layer was less resistant to the surfactant displacement.


Subject(s)
Emulsifying Agents/chemistry , Milk Proteins/chemistry , Drug Stability , Electrophoresis, Polyacrylamide Gel , Emulsions/chemistry , Ethylenediamines/chemistry , Hydrogen-Ion Concentration , Isoelectric Point , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Whey Proteins
6.
J Agric Food Chem ; 59(4): 1406-14, 2011 Feb 23.
Article in English | MEDLINE | ID: mdl-21247171

ABSTRACT

Whey protein isolate (WPI) was chemically modified by vanillic acid in order to enhance its cross-linkability by laccase enzyme. Incorporation of methoxyphenol groups created reactive sites for laccase on the surface of the protein and improved the efficiency of cross-linking. The vanillic acid modified WPI (Van-WPI) was characterized using MALDI-TOF mass spectrometry, and the laccase-catalyzed cross-linking of Van-WPI was studied. Furthermore, the vanillic acid modification was compared with the conventional approach to improve laccase-catalyzed cross-linking by adding free phenolic compounds. A small extent of the vanillic acid modification significantly improved the cross-linkability of the protein and made it possible to avoid color formation in a system that is free of small phenolic compounds. Moreover, the potential application of Van-WPI as emulsifier and the effect of cross-linking on the stability of Van-WPI emulsion were investigated. The post-emulsification cross-linking by laccase was proven to enhance the storage stability of Van-WPI emulsion.


Subject(s)
Cross-Linking Reagents/metabolism , Emulsifying Agents/chemistry , Laccase/metabolism , Milk Proteins/chemistry , Milk Proteins/metabolism , Emulsions/chemistry , Linseed Oil , Particle Size , Vanillic Acid/chemistry , Water , Whey Proteins
7.
J Agric Food Chem ; 57(8): 3316-24, 2009 Apr 22.
Article in English | MEDLINE | ID: mdl-19284754

ABSTRACT

Brewers' spent grain (BSG), a high-volume coproduct from the brewing industry, primarily contains proteins, barley cell wall carbohydrates, and lignin. To create new possibilities for the exploitation of this large biomass stream, the solubilization of BSG by the combined action of carbohydrases (Depol 740 and Econase) and peptidase (Alcalase and Promod 439) was explored. Hydrolysis protocols were optimized with respect to temperature (influencing both microbial contamination and rate of enzymatic hydrolysis), pH, enzyme dose, order of enzyme addition, and processing time. On the basis of this approach, one- and two-step protocols are proposed taking 4-8 h and yielding combined or separate fractions of hydrolyzed oligosaccharides and liberated hydrolyzed protein. Optimized procedures resulted in the solubilization of >80% of the proteinaceous material, up to 39% of the total carbohydrates, and up to 42% of total dry matter in BSG. Of the original xylan present in BSG, 36% could be solubilized. Sequential and simultaneous treatments with the two enzyme types gave similar results. In sequential processes, the order of the carbohydrase and peptidase treatments had only minor effects on the outcome. Depol 740 released more pentoses than Econase and gave slightly higher overall dry matter solubilization yields.


Subject(s)
Beer , Edible Grain/chemistry , Glycoside Hydrolases/metabolism , Hordeum/chemistry , Industrial Waste , Peptide Hydrolases/metabolism , Hydrolysis , Industrial Waste/analysis , Oligosaccharides/metabolism , Plant Proteins/metabolism , Solubility
8.
J Agric Food Chem ; 57(9): 3800-7, 2009 May 13.
Article in English | MEDLINE | ID: mdl-19326945

ABSTRACT

Sodium caseinate was chemically modified in order to alter its isoelectric point (pI). Negatively charged carboxylic groups were introduced to lower the pI, and positively charged amino groups to achieve the opposite. Different chemical amino acid modification approaches were studied and the modified proteins were characterized using free amino group assays, SDS-PAGE, MALDI-TOF mass spectrometry, and zeta potential measurements. Oil-in-water emulsions were prepared using these modified caseinates. The pH stability behavior of the emulsions was monitored, and interestingly, the stability of the emulsion could be modulated through steering the pI of caseinate. Using different modified caseinates, it was possible to create emulsions that were stable in the acid, neutral, and alkaline regions of the pH spectrum. The stability behavior of the emulsions correlated well with the theoretical and experimentally determined pI values of the caseinates. Storage stability of emulsions was also studied at pH values around 7, and emulsions made of modified caseinates showed storage stability similar to that of unmodified caseinate emulsions.


Subject(s)
Caseins/chemistry , Emulsifying Agents/chemistry , Chemical Phenomena , Drug Stability , Electrophoresis, Polyacrylamide Gel , Ethylenediamines/chemistry , Food Technology , Hydrogen-Ion Concentration , Isoelectric Point , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization , Succinic Anhydrides/chemistry
9.
J Agric Food Chem ; 56(14): 5717-22, 2008 Jul 23.
Article in English | MEDLINE | ID: mdl-18572915

ABSTRACT

Flaxseed oil was emulsified in whey protein isolate (WPI) and spray-dried. Powder characteristics and oxidative stability of oil at relative humidities (RH) from RH approximately 0% to RH 91% at 37 degrees C were analyzed. Oil droplets retained their forms in drying and reconstitution, but the original droplet size of the emulsion was not restored when the powder was dispersed in water. The particles seemed to be covered by a protein-rich surface layer as analyzed by electron spectroscopy for chemical analysis (ESCA). Oxidation of flaxseed oil dispersed in the WPI matrix was retarded from that of bulk oil but followed the same pattern as bulk oil with respect to humidity. A high rate of oxidation was found for both low and high humidity conditions. The lowest rate of oxidation as followed by peroxide values was found at RH 75%, a condition that is likely to diverge significantly from the monolayer moisture value. A weak baseline transition observed for the WPI matrix in a differential scanning calorimetry (DSC) thermogram suggested a glassy state of the matrix at all storage conditions. This was not consistent with the observed caking of the powder at RH 91%. Scanning electron microscopy (SEM) images revealed a considerable structural change in the WPI matrix in these conditions, which was suggested to be linked with a higher rate of oxygen transport. Possible mechanisms for oxygen transport in the whey protein matrix under variable RHs are discussed.


Subject(s)
Emulsions/chemistry , Humidity , Linseed Oil/chemistry , Milk Proteins/chemistry , Desiccation , Drug Stability , Food Preservation , Microscopy, Electron, Scanning , Oxidation-Reduction , Whey Proteins
10.
J Agric Food Chem ; 52(5): 1269-76, 2004 Mar 10.
Article in English | MEDLINE | ID: mdl-14995132

ABSTRACT

The stability of encapsulated D-limonene, which was prepared by spray drying, was studied in view of the release characteristics and oxidation stability. Gum arabic, soybean water-soluble polysaccharide, or modified starch, blended with maltodextrin were used as the wall materials. The powders were stored under the conditions of 23-96% relative humidity at 50 degrees C. The release rate and the oxidation rate were closely related to the relative humidity. The relationship was not simple. Initially, the release rate and the oxidation rate increased with increasing water activity, but around the glass transition temperature, the rates decreased sharply to increase again at a further increase of water activity. The results could be explained by a change in the powder structure, where a glass capsule matrix was changed into rubbery state during storage.


Subject(s)
Terpenes/chemistry , Water/chemistry , Capsules , Chemical Phenomena , Chemistry, Physical , Cyclohexenes , Desiccation , Drug Stability , Glass , Humidity , Limonene , Oxidation-Reduction , Temperature
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