Fractionation of Whey Protein Isolate with Supercritical Carbon Dioxide To Produce Enriched α-Lactalbumin and β-Lactoglobulin Food Ingredients

2012 ◽  
Vol 60 (20) ◽  
pp. 5257-5266 ◽  
Author(s):  
Laetitia M. Bonnaillie ◽  
Peggy M. Tomasula
2011 ◽  
Vol 13 (1) ◽  
pp. 240-259 ◽  
Author(s):  
Alexandra L. Yver ◽  
Laetitia M. Bonnaillie ◽  
Winnie Yee ◽  
Andrew McAloon ◽  
Peggy M. Tomasula

2014 ◽  
Vol 12 (3) ◽  
pp. 377-385 ◽  
Author(s):  
Vesna Šaponjac ◽  
Dragana Četojević-Simin ◽  
Gordana Ćetković ◽  
Jasna Čanadanović-Brunet ◽  
Sonja Djilas ◽  
...  

AbstractGround spice paprika was extracted with hexane, by conventional Soxhlet procedure (SX oleoresin), and with supercritical carbon dioxide at three different pressures — 20, 30 and 40 MPa (SF20, SF30 and SF40 oleoresins). The effect of extraction method and conditions on the colour intesity of paprika oleoresins, content of α-tocopherol, as well as antioxidant and antiproliferative activity was examined. Hexane showed highest selectivity for paprika pigments (886.02 ASTA), while α-tocopherol showed highest solubility (3846.9 mg kg−1) in supercritical carbon dioxide at 20 MPa. All paprika oleoresins exhibited good superoxide anion radical scavenging activity SF30 being the best superoxide anion radical scavenger. Cell growth activity was evaluated in vitro in human cell lines:cervix epitheloid carcinoma (HeLa), breast adenocarcinoma (MCF7) and colon adenocarcinoma (HT-29). The highest antiproliferative activity was exhibited by SX in MCF7 cell line (IC50=14.28 mg mL−1). Extract SF40 produced significant and selective antiproliferative action towards HeLa cell line. These results suggest that paprika oleoresins, due to high antiradical and tumor cell-inhibiting activity, can be regarded as functional food ingredients.


2020 ◽  
Vol 21 (15) ◽  
pp. 5544
Author(s):  
Rebecca Rabe ◽  
Ute Hempel ◽  
Laurine Martocq ◽  
Julia K. Keppler ◽  
Jenny Aveyard ◽  
...  

To improve the integration of a biomaterial with surrounding tissue, its surface properties may be modified by adsorption of biomacromolecules, e.g., fibrils. Whey protein isolate (WPI), a dairy industry by-product, supports osteoblastic cell growth. WPI’s main component, β-lactoglobulin, forms fibrils in acidic solutions. In this study, aiming to develop coatings for biomaterials for bone contact, substrates were coated with WPI fibrils obtained at pH 2 or 3.5. Importantly, WPI fibrils coatings withstood autoclave sterilization and appeared to promote spreading and differentiation of human bone marrow stromal cells (hBMSC). In the future, WPI fibrils coatings could facilitate immobilization of biomolecules with growth stimulating or antimicrobial properties.


Foods ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 625
Author(s):  
Sara Rebolleda ◽  
María Luisa González-San José ◽  
María Teresa Sanz ◽  
Sagrario Beltrán ◽  
Ángela G. Solaesa

A wheat bran oily extract obtained with supercritical carbon dioxide at 25.0 ± 0.1 MPa and 40 ± 2 °C has been analyzed in order to determine some valuable bioactive compounds as alkylresorcinols, α-linolenic acid, steryl ferulates, tocopherols and phenolic compounds, which levels were around 47, 37, 18, 7 and 0.025 mg/g oily extract, respectively. To our knowledge, this is the first time that the presence of steryl ferulates has been observed in a supercritical fluid extract of wheat bran and that γ-tocopherol has been described in wheat bran oily extracts. Other common quality parameters, directly correlated with oxidative degradation, were also evaluated. Acidity values around 15% oleic acid were detected, while low levels of hydroperoxides (around 2.4 meq O2/kg) and very low levels of hexanal (0.21 ppb) were found. Composition of the wheat bran oily extract was stable during 155 days of storage at 21 °C and darkness, and only a slight decrease in alkylresorcinols and tocopherols contents (13% and 20%, respectively) was observed. These results indicated an attractive potential of the obtained oily extract for industrial applications as food ingredients, nutraceuticals, and others.


2012 ◽  
Vol 80 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Katarina Lisak ◽  
Jose Toro-Sierra ◽  
Ulrich Kulozik ◽  
Rajka Božanić ◽  
Seronei Chelulei Cheison

The present study examines the resistance of the α-lactalbumin to α-chymotrypsin (EC 3.4.21.1) digestion under various experimental conditions. Whey protein isolate (WPI) was hydrolysed using randomised hydrolysis conditions (5 and 10% of WPI; pH 7·0, 7·8 and 8·5; temperature 25, 37 and 50 °C; enzyme-to-substrate ratio, E/S, of 0·1%, 0·5 and 1%). Reversed-phase high performance liquid chromatography (RP-HPLC) was used to analyse residual proteins. Heat, pH adjustment and two inhibitors (Bowman–Birk inhibitor and trypsin inhibitor from chicken egg white) were used to stop the enzyme reaction. While operating outside of the enzyme optimum it was observed that at pH 8·5 selective hydrolysis of β-lactoglobulin was improved because of a dimer-to-monomer transition while α-la remained relatively resistant. The best conditions for the recovery of native and pure α-la were at 25 °C, pH 8·5, 1% E/S ratio, 5% WPI (w/v) while the enzyme was inhibited using Bowman–Birk inhibitor with around 81% of original α-la in WPI was recovered with no more β-lg. Operating conditions for hydrolysis away from the chymotrypsin optimum conditions offers a great potential for selective WPI hydrolysis, and removal, of β-lg with production of whey protein concentrates containing low or no β-lg and pure native α-la. This method also offers the possibility for production of β-lg-depleted milk products for sensitive populations.


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