Noncovalent interaction of cyanidin-3-O-glucoside with whey protein isolate and β-lactoglobulin: Focus on fluorescence quenching and antioxidant properties

LWT ◽  
2021 ◽  
Vol 137 ◽  
pp. 110386
Author(s):  
Yueyue Meng ◽  
Linlin Hao ◽  
Ying Tan ◽  
Yuzhuo Yang ◽  
Libo Liu ◽  
...  
Keyword(s):  
Fluorescence Quenching ◽  
Whey Protein ◽  
Antioxidant Properties ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Noncovalent Interaction ◽  
Β Lactoglobulin

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 ◽  
...  
Keyword(s):  
Whey Protein ◽  
Antimicrobial Properties ◽  
Whey Protein Isolate ◽  
Protein Isolate ◽  
Surrounding Tissue ◽  
Osteoblastic Cell ◽  
Bone Contact ◽  
Acidic Solutions ◽  
Main Component ◽  
Β Lactoglobulin

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.

Chymotrypsin selectively digests β-lactoglobulin in whey protein isolate away from enzyme optimal conditions: Potential for native α-lactalbumin purification

2012 ◽  
Vol 80 (1) ◽  
pp. 14-20 ◽  
Author(s):  
Katarina Lisak ◽  
Jose Toro-Sierra ◽  
Ulrich Kulozik ◽  
Rajka Božanić ◽  
Seronei Chelulei Cheison
Keyword(s):  
Whey Protein ◽  
High Performance ◽  
Enzyme Reaction ◽  
Whey Protein Isolate ◽  
Reversed Phase ◽  
Protein Isolate ◽  
Operating Conditions ◽  
Selective Hydrolysis ◽  
Experimental Conditions ◽  
Β Lactoglobulin

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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