scholarly journals Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils

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.

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.


Foods ◽  
2021 ◽  
Vol 10 (2) ◽  
pp. 401
Author(s):  
Maria-Ioana Socaciu ◽  
Melinda Fogarasi ◽  
Elemér Lajos Simon ◽  
Cristina Anamaria Semeniuc ◽  
Sonia Ancuţa Socaci ◽  
...  

The efficiency of some films prepared from heat-denatured whey protein isolate solutions on the quality and shelf-life of brook trout samples during storage at 4 °C was studied in this research (WPIf-a film based on whey protein isolate and WPIf+2.5%TEO-a film based on whey protein isolate incorporated with 2.5% tarragon essential oil). The control and covered fish samples were periodically assessed (at 3 days) over 15 days of storage for the physicochemical (pH; EC, electrical conductivity; TVB-N, total volatile basic nitrogen; TBARS, thiobarbituric acid reactive substances; color), microbiological (TVC, total viable count; PTC, psychrotrophic count; LAB, lactic acid bacteria; H2S-producing bacteria), and sensory properties (color discoloration; odor; overall acceptability). The WPIf+2.5%TEO has proven enhanced quality preservation effects compared to WPIf by showing lower values for physicochemical parameters, lower microbial loads, and higher sensory scores in the fish sample. All these effects have led to an extension of the sample’s shelf-life. In conclusion, the tarragon essential oil has conferred antioxidant and antimicrobial properties to the film. Thus, the WPIf+2.5%TEO could be a promising material for the packaging of fresh brook trout during refrigerated storage.


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