Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2022 Mar 14;11(6):829.
doi: 10.3390/foods11060829.

The Influence of Whey Protein Heating Parameters on Their Susceptibility to Digestive Enzymes and the Antidiabetic Activity of Hydrolysates

Affiliations

The Influence of Whey Protein Heating Parameters on Their Susceptibility to Digestive Enzymes and the Antidiabetic Activity of Hydrolysates

Kungnang Bunsroem et al. Foods. .

Abstract

The inhibition of dipeptidyl peptidase-IV (DPP-IV) and the release of glucagon-like peptide-1 (GLP-1) could normalize blood glucose levels in diabetic patients. This study evaluated the susceptibility of whey proteins to enzyme hydrolysis and the antidiabetic properties of protein hydrolysates from β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) solutions compared with whey protein isolate (WPI) solution treated at different heating temperatures (65, 75, and 85 °C). α-LA hydrolysate provided the lowest degree of hydrolysis (DH). Those heating temperatures did not significantly affect the DH of all protein hydrolysates. α-LA hydrolysate significantly increased GLP-1 levels and DPP-IV inhibitory activity more than β-LG hydrolysate. WPI hydrolysate inhibited DPP-IV activity less than an α-LA hydrolysate, but they were no significant differences for GLP-1 release activity. Heat treatment could affect the antidiabetic properties of all protein hydrolysates. Heating at 75 °C resulted in greater inhibition of the activity of DPP-IV than at 65 and 85 °C. The highest increase in GLP-1 release was also observed by heating at 75 °C. The recently obtained information is useful for the utilization of α-LA, heated at 75 °C for 30 min, in the preparation of antidiabetic food supplements.

Keywords: antidiabetic; heat treatment; whey protein; α-lactalbumin; β-lactoglobulin.

PubMed Disclaimer

Conflict of interest statement

The authors declare no conflict of interest. The funders had no role in the design of the study; in the collection, analyses, or interpretation of data; in the writing of the manuscript, or in the decision to publish the results.

Figures

Figure 1
Figure 1
Degree of hydrolysis (DH, %) of protein hydrolysates: (a) Comparisons between different types of protein solutions (WPI, β-LG, and α-LA), and (b) comparisons between different heat treatment temperatures (65, 75, and 85 °C) for 30 min for all protein solutions. Data are presented as mean ± standard deviation (n = 3). The different letters A,B indicate a significant difference at p < 0.05. The letter ns indicates no significant difference at p ≥ 0.05. WPI, β-LG, and α-LA denote whey protein isolate, β-lactoglobulin, and α-lactalbumin, respectively.
Figure 2
Figure 2
Cell viability (%) of the human salivary gland (HSG) cells after 24 h incubation with DMEM (control) and the protein hydrolysate at concentrations between 0.078 and 10 mg/mL (n = 4). WPI, LG, and LA denote whey protein isolate, β-lactoglobulin, and α-lactalbumin solutions, respectively. The number after the abbreviated protein solutions indicates the temperature (°C) of the heat treatment process.
Figure 3
Figure 3
Dipeptidyl peptidase-IV (DPP-IV) inhibition values (%) of protein hydrolysates at a concentration of 0.313 mg/mL: (a) Comparisons between different types of protein hydrolysates from WPI, β-LG, and α-LA solutions; (b) comparisons between different heat treatment temperatures (65, 75, and 85 °C) for 30 min for all protein hydrolysates. Data are presented as mean ± standard deviation (n = 3). The different letters A,B indicate a significant difference at p < 0.05. WPI, β-LG, and α-LA denote whey protein isolate, β-lactoglobulin, and α-lactalbumin, respectively.
Figure 4
Figure 4
Bi-plot for the protein hydrolysates and their properties from principal component analysis (PCA). WPI, LG, and LA denote whey protein isolate, β-lactoglobulin, and α-lactalbumin solutions, respectively. The number after the abbreviated protein solutions indicate the temperature (°C) of the heat treatment process.

Similar articles

Cited by

References

    1. Wang P.-C., Zhao S., Yang B.-Y., Wang Q.-H., Kuang H.-X. Anti-diabetic polysaccharides from natural sources: A review. [(accessed on 20 August 2021)];Carbohydr. Polym. 2016 148:86–97. doi: 10.1016/j.carbpol.2016.02.060. Available online: http://www.sciencedirect.com/science/article/pii/S0144861716301254. - DOI - PubMed
    1. Olesen K., Cleal B., Willaing I. Discrimination and stigma among people with type 2 diabetes in the workplace: Prejudice against illness or obesity? [(accessed on 20 August 2021)];Public Health. 2020 180:100–101. doi: 10.1016/j.puhe.2019.11.009. Available online: http://www.sciencedirect.com/science/article/pii/S003335061930366X. - DOI - PubMed
    1. Omar B., Ahrén B. Pleiotropic Mechanisms for the Glucose-Lowering Action of DPP-4 Inhibitors. [(accessed on 20 August 2021)];Diabetes. 2014 63:2196–2202. doi: 10.2337/db14-0052. Available online: http://diabetes.diabetesjournals.org/content/63/7/2196.abstract. - DOI - PubMed
    1. Zhang B.B., Zhou G., Li C. AMPK: An Emerging Drug Target for Diabetes and the Metabolic Syndrome. [(accessed on 20 August 2021)];Cell Metab. 2009 9:407–416. doi: 10.1016/j.cmet.2009.03.012. Available online: https://www.sciencedirect.com/science/article/pii/S1550413109000904. - DOI - PubMed
    1. Andrade J., Pereira C.G., Junior J.C.D.A., Viana C.C.R., Neves L.N.D.O., da Silva P.H.F., Bell M.J.V., Anjos V.D.C.D. FTIR-ATR determination of protein content to evaluate whey protein concentrate adulteration. [(accessed on 23 August 2021)];LWT. 2019 99:166–172. doi: 10.1016/j.lwt.2018.09.079. Available online: http://www.sciencedirect.com/science/article/pii/S0023643818308107. - DOI

LinkOut - more resources