Protein Concentrates

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Joyce I Boye - One of the best experts on this subject based on the ideXlab platform.

  • in vitro Protein digestibility and physico chemical properties of flours and Protein Concentrates from two varieties of lentil lens culinaris
    Food & Function, 2013
    Co-Authors: Chockry Barbana, Joyce I Boye
    Abstract:

    The chemical composition of whole lentil flours and lentil Protein Concentrates prepared by alkaline extraction and iso-electric precipitation from Blaze and Laird varieties of lentil were studied. The Protein composition of the flours and Concentrates, determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) and size-exclusion high-performance liquid chromatography (SE-HPLC) showed that the extracted Proteins were composed mainly of globulins and albumins. Trypsin inhibitor activity ranged between 0.94 and 1.94 trypsin inhibitor units (TIU) mg−1 for the flours, but was markedly lower in the Protein Concentrates ranging between 0.17 and 0.66 TIU mg−1. In vitro Protein digestibility ranged between 75.90 and 77.05% for the flours, whereas significantly (P < 0.05) higher values, ∼82.80 to 83.20%, were determined for the Concentrates. Significant (P < 0.05) differences in colour (ΔE) were observed between the flours and the Concentrates from both varieties. Thermal properties of both flours as studied by differential scanning calorimetry (DSC) were comparable. However, the endothermic parameters of the two Protein Concentrates were significantly (P < 0.05) different. Overall, the results show that in vitro Protein digestibility of lentil Protein Concentrates is higher than that of the flours, however, both lentil flours and Protein Concentrates contain useful Proteins that could serve as value-added ingredients in food formulations.

  • In vitro binding of bile salts by lentil flours, lentil Protein Concentrates and lentil Protein hydrolysates
    Food Research International, 2011
    Co-Authors: Chockry Barbana, Anne Claire Boucher, Joyce I Boye
    Abstract:

    Abstract The binding capacity of bile salts by lentil flours produced from two varieties, Blaze and Laird and their Protein Concentrates and hydrolysates were studied. Sodium cholate, sodium deoxycholate, sodium taurocholate, sodium glycocholate and sodium chenodeoxycholate were tested individually, and their binding interactions with the lentil products were analyzed using the Trinity Biotech Bile Acids Kit 450-10 and compared to cholestyramine. All tested samples bound the bile salts investigated, and the amount of bile salts bound (> 70%) was sometimes greater than that bound by cholestyramine. Overall, there were no major differences in the bile salt binding capacities of similar samples prepared from the two varieties of lentil. In vitro digestion of the lentil Proteins by pepsin/trypsin/α-chymotrypsin, alcalase/flavourzyme and papain significantly reduced the bile salt binding capacity compared to the undigested samples except in the case of sodium deoxycholate where no significant differences in bile salt binding were observed before and after hydrolysis. Binding of bile salts has been linked to cholesterol reduction, thus, the ability of the lentil products to bind bile salts is of interest as it may suggest that lentils could potentially have cholesterol-reducing properties.

  • influence of processing on composition and antinutritional factors of chickpea Protein Concentrates produced by isoelectric precipitation and ultrafiltration
    Innovative Food Science and Emerging Technologies, 2009
    Co-Authors: Martin Mondor, Helene Drolet, Salih Aksay, Samira Roufik, Edward R Farnworth, Joyce I Boye
    Abstract:

    Abstract The effect of chickpea processing (i.e. defatting, isoelectric precipitation vs ultrafiltration/diafiltration) on the composition, Protein recovery and antinutritional factors of Protein Concentrates was studied for two varieties (Mylese and Xena). Defatting did not affect significantly the content of antinutritional factors in the flours. However, production of Concentrates from defatted flours by isoelectric precipitation resulted in higher phosphorous and phenolic contents compared to the Concentrates produced by the same process using the full fat flours as starting material, while trypsin inhibitor content was not affected. When processed by ultrafiltration/diafiltration, Protein Concentrates produced from defatted flour showed a slightly lower trypsin inhibitor content than the ones produced from full fat flours in most cases, while the inverse was true for the phosphorous content, and for the phenolic content; this effect was a function of chickpea variety. Overall, UF pH 9/DF pH 6 resulted in Concentrates with the lowest phosphorous content, while isoelectric precipitation and UF pH 9/DF pH 9 resulted in Concentrates with lower phenolic content compared to the ones produced by UF pH 9/DF pH 6; for both processes the trypsin inhibitor content of the Concentrates remained high. Industrial relevance Chickpea production is one of the major agricultural sectors of significant importance to Canada. Although chickpeas are grown in Canada for export, very little is exported in the value-added or processed form. Development of new extraction technologies and value-added products such as the ones presented in this paper is of interest for Canada since it would have a significant impact on the growth of the industry domestically, thus, creating opportunities to strengthen rural development in Canada. Successful implementation of these technologies would make interested Canadian companies viable competitors in the global plant Protein production industry and would put Canada in a good position to enjoy a large share of this market both locally and internationally. More specifically, we are the first research group to compare the use of isoelectric precipitation and ultrafiltration/diafiltration for the production of chickpea Protein Concentrates from full fat and defatted flours of Kabuli and Desi chickpea variety, and to quantify the effect of these processes on the composition and on the antinutritional factors (i.e. phytic acid, total phenolics and trypsin inhibitors) of the resulting Concentrates. Overall, it was observed that isoelectric precipitation was effective to an extent in producing Concentrates with low phosphorous and phenolic contents. UF pH 9/DF pH 9 was also effective to an extent in producing Concentrates with low phenolic content, while UF pH 9/DF pH 6 was more efficient in producing Concentrates with low phosphorous content. High-quality chickpea Protein Concentrates with improved nutritional properties and good functional properties could beneficially be combined with other Protein sources, such as soy Protein, or be used in the formulation of foods, such as meat analogues, dairy, and bakery products.

Jingshun Zhang - One of the best experts on this subject based on the ideXlab platform.

  • multiple reaction monitoring based determination of bovine α lactalbumin in infant formulas and whey Protein Concentrates by ultra high performance liquid chromatography tandem mass spectrometry using tryptic signature peptides and synthetic peptide
    Analytica Chimica Acta, 2012
    Co-Authors: Jingshun Zhang, Baifen Huang, Shiyun Lai, Yu Zhang, Yiping Ren
    Abstract:

    The determination of α-lactalbumin in various dairy products attracts wide attention in multidiscipline fields because of its nutritional and biological functions. In the present study, we quantified the bovine α-lactalbumin in various infant formulas and whey Protein Concentrates using ultra-high performance liquid chromatography coupled to tandem mass spectrometer in multiple reaction monitoring mode. Bovine α-lactalbumin was quantified by employing the synthetic internal standard based on the molar equivalent relationship among the internal standard, bovine α-lactalbumin and their signature peptides. This study especially focused on the recovery rates of the sample preparation procedure and robust quantification of total bovine α-lactalbumin in its native and thermally denatured form with a synthetic internal standard KILDKVGINNYWLAHKALCSE. The observed recovery rates of bovine α-lactalbumin ranged from 95.8 to 100.6% and the reproducibility was excellent (RSD<6%) at different spiking levels. The limit of quantitation is 10 mg/100 g for infant formulas and whey Protein Concentrates. In order to validate the applicability of the method, 21 brands of infant formulas were analyzed. The acquired contents of bovine α-lactalbumin were 0.67-1.84 g/100g in these infant formulas in agreement with their label claimed values. The experiment of heat treatment time showed that the loss of native α-lactalbumin enhanced with an increasing intensity of heat treatment. Comparing with Ren's previous method by analysis of only native bovine α-lactalbumin, the present method at the peptide level proved to be highly suitable for measuring bovine α-lactalbumin in infant formulas and whey Protein Concentrates, avoiding forgoing the thermally induced denatured α-lactalbumin caused by the technological processing.

  • determination of disialoganglioside gd3 and monosialoganglioside gm3 in infant formulas and whey Protein Concentrates by ultra performance liquid chromatography electrospray ionization tandem mass spectrometry
    IEEE Journal of Solid-state Circuits, 2012
    Co-Authors: Jingshun Zhang, Baifen Huang, Marlene Ransborg Pedersen, Duo Li
    Abstract:

    : A method of ultra-performance liquid chromatography combined with electrospray ionization triple quadrupole tandem mass spectrometry (UPLC-ESI-MS/MS) has been established for simultaneous determination of major disialoganglioside 3 (GD3) and monosialoganglioside 3 (GM3) in infant formulas and whey Protein Concentrates. Gangliosides were extracted by using the technique of Svennerholm and Fredman and then cleaned up with OASIS HLB solid-phase extraction (SPE) cartridges. The various molecular species of gangliosides were separated on an Acquity UPLC BEH C8 column and analyzed under the negative ion mode. GD3 and GM3 were rapidly quantified using internal standard (IS) method. The developed method was further validated by determining the linearity, average recovery, sensitivity (limit of quantification), and precision. The results presented high correlation coefficients (R(2) > 0.993) of the selected 16 gangliosides molecular species and provided the respective linear ranges. The limit of quantification was 0.325-0.734 mg/100 g for eight molecular species of GD3 and 0.008-0.312 mg/100 g for eight molecular species of GM3, respectively. The reasonable average recoveries (81-95%) and precision (relative standard deviation [RSD] ≤15%) were also demonstrated in three different spiked levels. This new method would be very useful in the quantitative determination of gangliosides in infant formulas and whey Protein Concentrates.

Duo Li - One of the best experts on this subject based on the ideXlab platform.

  • determination of disialoganglioside gd3 and monosialoganglioside gm3 in infant formulas and whey Protein Concentrates by ultra performance liquid chromatography electrospray ionization tandem mass spectrometry
    IEEE Journal of Solid-state Circuits, 2012
    Co-Authors: Jingshun Zhang, Baifen Huang, Marlene Ransborg Pedersen, Duo Li
    Abstract:

    : A method of ultra-performance liquid chromatography combined with electrospray ionization triple quadrupole tandem mass spectrometry (UPLC-ESI-MS/MS) has been established for simultaneous determination of major disialoganglioside 3 (GD3) and monosialoganglioside 3 (GM3) in infant formulas and whey Protein Concentrates. Gangliosides were extracted by using the technique of Svennerholm and Fredman and then cleaned up with OASIS HLB solid-phase extraction (SPE) cartridges. The various molecular species of gangliosides were separated on an Acquity UPLC BEH C8 column and analyzed under the negative ion mode. GD3 and GM3 were rapidly quantified using internal standard (IS) method. The developed method was further validated by determining the linearity, average recovery, sensitivity (limit of quantification), and precision. The results presented high correlation coefficients (R(2) > 0.993) of the selected 16 gangliosides molecular species and provided the respective linear ranges. The limit of quantification was 0.325-0.734 mg/100 g for eight molecular species of GD3 and 0.008-0.312 mg/100 g for eight molecular species of GM3, respectively. The reasonable average recoveries (81-95%) and precision (relative standard deviation [RSD] ≤15%) were also demonstrated in three different spiked levels. This new method would be very useful in the quantitative determination of gangliosides in infant formulas and whey Protein Concentrates.

Peter C K Cheung - One of the best experts on this subject based on the ideXlab platform.

Raymond L. Legge - One of the best experts on this subject based on the ideXlab platform.

  • functional properties of navy bean phaseolus vulgaris Protein Concentrates obtained by pneumatic tribo electrostatic separation
    Food Chemistry, 2019
    Co-Authors: Solmaz Tabtabaei, Dinara Konakbayeva, Amin Reza Rajabzadeh, Raymond L. Legge
    Abstract:

    Abstract A sustainable, chemical-free dry tribo-electrostatic separation approach was employed to fractionate navy bean flour. The resulting Protein-enriched fractions had 36–38% Protein on a moisture free basis, accounting for 43% of the total available Protein. SDS-PAGE analysis of the dry-enriched Protein fractions showed a similar Protein profile to that of the original navy bean flour. The functional properties of these fractions were examined and compared with the commercial soybean Protein concentrate as well as navy bean Protein isolate obtained by a conventional wet fractionation process. These electrostatically separated Protein fractions exhibited superior solubility at their intrinsic pH as well as superior emulsion stability (ES), foam expansion (FE) and foam volume stability (FVS) compared to the wet-fractionated navy bean Protein isolate that was almost depleted of albumins, exhibiting poor solubility and foaming properties. These results suggest electrostatic separation as a promising route to deliver functional Protein Concentrates as novel food formulation ingredients.