Dataset Information

Molecular Properties of Flammulina velutipes Polysaccharide-Whey Protein Isolate (WPI) Complexes via Noncovalent Interactions.

ABSTRACT: Whey protein isolate (WPI) has a variety of nutritional benefits. The stability of WPI beverages has attracted a large amount of attention. In this study, Flammulina velutipes polysaccharides (FVPs) interacted with WPI to improve the stability via noncovalent interactions. Multiple light scattering studies showed that FVPs can improve the stability of WPI solutions, with results of radical scavenging activity assays demonstrating that the solutions of the complex had antioxidant activity. The addition of FVPs significantly altered the secondary structures of WPI, including its ?-helix and random coil. The results of bio-layer interferometry (BLI) analysis indicated that FVPs interacted with the WPI, and the equilibrium dissociation constant (K_D) was calculated as 1.736 × 10^-4 M in this study. The in vitro digestibility studies showed that the FVPs protected WPI from pepsin digestion, increasing the satiety. Therefore, FVPs effectively interact with WPI through noncovalent interactions and improve the stability of WPI, with this method expected to be used in protein-enriched and functional beverages.

SUBMITTER: Shang J

PROVIDER: S-EPMC7821936 | biostudies-literature | 2020 Dec

REPOSITORIES: biostudies-literature

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Publications

Molecular Properties of <i>Flammulina velutipes</i> Polysaccharide-Whey Protein Isolate (WPI) Complexes via Noncovalent Interactions.

Shang Jiaqi J Liao Minhe M Jin Ritian R Teng Xiangyu X Li Hao H Xu Yan Y Zhang Ligang L Liu Ning N

Foods (Basel, Switzerland) 20201222 1

Whey protein isolate (WPI) has a variety of nutritional benefits. The stability of WPI beverages has attracted a large amount of attention. In this study, <i>Flammulina velutipes</i> polysaccharides (FVPs) interacted with WPI to improve the stability via noncovalent interactions. Multiple light scattering studies showed that FVPs can improve the stability of WPI solutions, with results of radical scavenging activity assays demonstrating that the solutions of the complex had antioxidant activity. ...[more]

PMID: 33374899

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Project description:Multilayer plastic films provide a range of properties, which cannot be obtained from monolayer films but, at present, their recyclability is an open issue and should be improved. Research to date has shown the possibility of using whey protein as a layer material with the property of acting as an excellent barrier against oxygen and moisture, replacing petrochemical non-recyclable materials. The innovative approach of the present research was to achieve the recyclability of the substrate films by separating them, with a simple process compatible with industrial procedures, in order to promote recycling processes leading to obtain high value products that will beneficially impact the packaging and food industries. Hence, polyethyleneterephthalate (PET)/polyethylene (PE) multi-layer film was prepared based on PET coated with a whey protein layer, and then the previous structure was laminated with PE. Whey proteins, constituting the coating, can be degraded by enzymes so that the coating films can be washed off from the plastic substrate layer. Enzyme types, dosage, time, and temperature optima, which are compatible with procedures adopted in industrial waste recycling, were determined for a highly-efficient process. The washing of samples based on PET/whey and PET/whey/PE were efficient when performed with enzymatic detergent containing protease enzymes, as an alternative to conventional detergents used in recycling facilities. Different types of enzymatic detergents tested presented positive results in removing the protein layer from the PET substrate and from the PET/whey/PE multilayer films at room temperature. These results attested to the possibility of organizing the pre-treatment of the whey-based multilayer film by washing with different available commercial enzymatic detergents in order to separate PET and PE, thus allowing a better recycling of the two different polymers. Mechanical properties of the plastic substrate, such as stress at yield, stress and elongation at break, evaluated by tensile testing on films before and after cleaning, were are not significantly affected by washing with enzymatic detergents.

Dataset Information

Molecular Properties of Flammulina velutipes Polysaccharide-Whey Protein Isolate (WPI) Complexes via Noncovalent Interactions.

Publications

Molecular Properties of <i>Flammulina velutipes</i> Polysaccharide-Whey Protein Isolate (WPI) Complexes via Noncovalent Interactions.

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