scholarly journals Use of Whey Protein as a Natural Polymer for Tissue Adhesive: Preliminary Formulation and Evaluation In Vitro

Polymers ◽  
2018 ◽  
Vol 10 (8) ◽  
pp. 843 ◽  
Author(s):  
Guorong Wang ◽  
Ning Liu ◽  
Mingruo Guo
Keyword(s):  
Whey Protein ◽  
Protein A ◽  
Protein Isolate ◽  
Tissue Adhesive ◽  
Potential Candidate ◽  
Air Leakage ◽  
Scarless Surgery ◽  
The Usa ◽  
Β Lactoglobulin

The use of sutures is still the most widely practiced solution for wound closure and tissue reconstruction; however, scarring is a common defect resulting from sutures on topical use. In some cases, the conventional sutures are unable to seal the sites where fluid and air leakage could occur. Tissue adhesives though have lower tensile strength than sutures, may make scarless surgery possible, or prevent fluid and air leakage. A product called BioGlue® (CryoLife Inc, Kennesaw, GA, USA), based on bovine serum albumin (BSA, a protein) and glutaraldehyde (GTA, crosslinker), has been approved for clinical use in the USA. Whey protein, a byproduct of cheese-making, comprised mainly of β-lactoglobulin, α-lactalbumin and BSA. Even though the molecular weight of BSA is about three times larger than the molecular of β-lactoglobulin and α-lactalbumin, all three proteins are rich in free ε-amino groups (can react with GTA) and globular proteins. This similarity make whey protein a potential candidate to replace BSA in the tissue adhesive since whey protein is abundant and much cheaper than BSA. In this study, whey protein isolate (WPI) was used as a protein polymer with GTA as a crosslinker to evaluate the feasibility of whey protein for tissue adhesive formulation. Results showed that the WPI/GTA adhesive exhibited a comparable adhesive strength to BioGlue® control.

scholarly journals Physicochemical and Microstructural Characterization of Whey Protein Films Formed with Oxidized Ferulic/Tannic Acids

Foods ◽  
2021 ◽  
Vol 10 (7) ◽  
pp. 1599
Author(s):  
Yaosong Wang ◽  
Youling L. Xiong
Keyword(s):  
Whey Protein ◽  
Microstructural Characterization ◽  
Protein Isolate ◽  
Light Transmittance ◽  
In Vitro Digestibility ◽  
Protein Films ◽  
Film Forming ◽  
Protein Sulfhydryl ◽  
Reduced Light

Protein-based biodegradable packaging films are of environmental significance. The effect of oxidized ferulic acid (OFA)/tannic acid (OTA) on the crosslinking and film-forming properties of whey protein isolate (WPI) was investigated. Both of the oxidized acids induced protein oxidation and promoted WPI crosslinking through the actions of quinone carbonyl and protein sulfhydryl, and amino groups. OTA enhanced the tensile strength (from 4.5 MPa to max 6.7 MPa) and stiffness (from 215 MPa to max 376 MPa) of the WPI film, whereas OFA significantly increased the elongation at break. The water absorption capability and heat resistance of the films were greatly improved by the addition of OTA. Due to the original color of OTA, the incorporation of OTA significantly reduced light transmittance of the WPI film (λ 200–600 nm) as well as the transparency, whereas no significant changes were induced by the OFA treatment. Higher concentrations of OTA reduced the in vitro digestibility of the WPI film, while the addition of OFA had no significant effect. Overall, these two oxidized polyphenols promoted the crosslinking of WPI and modified the film properties, with OTA showing an overall stronger efficacy than OFA due to more functional groups available.

scholarly journals Exploring the Use of a Modified High-Temperature, Short-Time Continuous Heat Exchanger with Extended Holding Time (HTST-EHT) for Thermal Inactivation of Trypsin Following Selective Enzymatic Hydrolysis of the β-Lactoglobulin Fraction in Whey Protein Isolate

Foods ◽  
2019 ◽  
Vol 8 (9) ◽  
pp. 367 ◽  
Author(s):  
Laura Sáez ◽  
Eoin Murphy ◽  
Richard J. FitzGerald ◽  
Phil Kelly
Keyword(s):  
High Temperature ◽  
Heat Exchanger ◽  
Whey Protein ◽  
Protein Isolate ◽  
Holding Time ◽  
High Temperature Short Time ◽  
Incubation Periods ◽  
Short Time ◽  
Β Lactoglobulin ◽  
Hydrolysis Of

Tryptic hydrolysis of whey protein isolate under specific incubation conditions including a relatively high enzyme:substrate (E:S) ratio of 1:10 is known to preferentially hydrolyse β-lactoglobulin (β-LG), while retaining the other major whey protein fraction, i.e., α-lactalbumin (α-LA) mainly intact. An objective of the present work was to explore the effects of reducing E:S (1:10, 1:30, 1:50, 1:100) on the selective hydrolysis of β-LG by trypsin at pH 8.5 and 25 °C in a 5% (w/v) WPI solution during incubation periods ranging from 1 to 7 h. In addition, the use of a pilot-scale continuous high-temperature, short-time (HTST) heat exchanger with an extended holding time (EHT) of 5 min as a means of inactivating trypsin to terminate hydrolysis was compared with laboratory-based acidification to <pH 3 by the addition of HCl, and batch sample heating in a water bath at 85 °C. An E:S of 1:10 resulted in 100% and 30% of β-LG and α-LA hydrolysis, respectively, after 3 h, while an E:S reduction to 1:30 and 1:50 led >90% β-LG hydrolysis after respective incubation periods of 4 and 6 h, with <5% hydrolysis of α-LA in the case of 1:50. Continuous HTST-EHT treatment was shown to be an effective inactivation process allowing for the maintenance of substrate selectivity. However, HTST-EHT heating resulted in protein aggregation, which negatively impacts the downstream recovery of intact α-LA. An optimum E:S was determined to be 1:50, with an incubation time ranging from 3 h to 7 h leading to 90% β-LG hydrolysis and minimal degradation of α-LA. Alternative batch heating by means of a water bath to inactivate trypsin caused considerable digestion of α-LA, while acidification to <pH 3.0 restricted subsequent functional applications of the protein.

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.

Comparison of the ability to bind lipids of β-lactoglobulin and serum albumin of milk from ruminant and non-ruminant species

1993 ◽  
Vol 60 (1) ◽  
pp. 55-63 ◽  
Author(s):  
M. Dolores Pérez ◽  
Pilar Puyol ◽  
José Manuel Ena ◽  
Miguel Calvo
Keyword(s):  
Fatty Acids ◽  
Guinea Pig ◽  
Serum Albumin ◽  
Whey Protein ◽  
Whey Proteins ◽  
Gel Filtration ◽  
Ruminant Species ◽  
Β Lactoglobulin

SummaryThe interaction of sheep, horse, pig, human and guinea-pig whey proteins with fatty acids has been studied. Using gel filtration and autoradiography, it was found that sheep β-lactoglobulin and serum albumin from all species had the ability to bind fatty acids in vitro. Sheep β-lactoglobulin, isolated from milk, had ˜ 0·5 mol fatty acids bound per mol monomer protein, and albumin from sheep, horse and pig contained ˜ 4·5, 2·9 and 4·7 mol fatty acids/mol protein respectively. However, β-lactoglobulin from horse and pig milk had neither fatty acids physiologically bound nor the ability to bind them in vitro. Albumin was the only whey protein detected with bound fatty acids in these species as well as in human and guinea pig. This suggests that the ability of ruminant β-lactoglobulin to bind fatty acids was not shared by the same protein of non-ruminants.

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