Development of lentil peptides with potent antioxidant, antihypertensive, and antidiabetic activities along with umami taste

doi:10.1002/fsn3.3279

. 2023 Feb 27;11(6):2974-2989.

doi: 10.1002/fsn3.3279. eCollection 2023 Jun.

Development of lentil peptides with potent antioxidant, antihypertensive, and antidiabetic activities along with umami taste

Amir Rezvankhah ¹, Mohammad Saeid Yarmand ¹, Babak Ghanbarzadeh ², Homaira Mirzaee ³

Affiliations

¹ Department of Food Science and Technology, Razi Food Chemistry Lab College of Agriculture and Natural Resources, University of Tehran Karaj Iran.
² Department of Food Science and Technology, Faculty of Agriculture University of Tabriz Tabriz Iran.
³ Department of Food Science and Technology, Faculty of Agriculture Tarbiat Modares University Tehran Iran.

PMID: 37324857
PMCID: PMC10261806
DOI: 10.1002/fsn3.3279

Development of lentil peptides with potent antioxidant, antihypertensive, and antidiabetic activities along with umami taste

Amir Rezvankhah et al. Food Sci Nutr. 2023.

. 2023 Feb 27;11(6):2974-2989.

doi: 10.1002/fsn3.3279. eCollection 2023 Jun.

Authors

Amir Rezvankhah ¹, Mohammad Saeid Yarmand ¹, Babak Ghanbarzadeh ², Homaira Mirzaee ³

Affiliations

¹ Department of Food Science and Technology, Razi Food Chemistry Lab College of Agriculture and Natural Resources, University of Tehran Karaj Iran.
² Department of Food Science and Technology, Faculty of Agriculture University of Tabriz Tabriz Iran.
³ Department of Food Science and Technology, Faculty of Agriculture Tarbiat Modares University Tehran Iran.

PMID: 37324857
PMCID: PMC10261806
DOI: 10.1002/fsn3.3279

Abstract

Lentil peptides have shown promising bioactive properties regarding the antioxidant activity and also inhibitory activity of angiotensin-I-converting enzyme (ACE). Sequential hydrolysis of proteins has shown a higher degree of hydrolysis with enhanced antioxidant and ACE-inhibitory activities. The lentil protein concentrate (LPC) was sequentially hydrolyzed using Alcalase and Flavourzyme at 2% w/w. The hydrolysate (LPH) was cross-linked (LPHC) or sonicated (LPHUS) and sequentially cross-linked (LPHUSC). Amino acid profile, molecular weight (MW) distribution, DPPH and ABTS radical scavenging activities (RSA; 7 mg/mL), ACE (0.1-2 mg/mL), α-glucosidase, and α-amylase inhibitory activities (10-500 μg/mL), and umami taste were determined. The highest DPPH RSA was obtained for LPH (68.75%), followed by LPHUSC (67.60%), and LPHUS (67.49%) while the highest ABTS RSA values were obtained for LPHC (97.28%) and LPHUSC (97.20%). Cross-linking and sonication led to the improvement of the ACE-inhibitory activity so that LPHUSC and LPHC had IC₅₀ values of 0.23 and 0.27 mg/mL, respectively. LPHC and LPHUSC also indicated higher α-glucosidase inhibitory activity (IC50 of 1.2 and 1.23 mg/mL) compared to LPH (IC50 of 1.74 mg/mL) and LPHUS (IC50 of 1.75 mg/mL) while the IC50 value of acarbose indicated 0.51 mg/mL. Moreover, LPHC and LPHUSC exhibited higher α-amylase inhibitory activities (IC50 of 1.35 and 1.16 mg/mL) than LPHUS (IC50 of 1.95 mg/mL), and LPH (IC50 of 2.51 mg/mL) while acarbose had an IC50 value of 0.43 mg/mL. Umami taste analysis revealed that LPH and LPHC due to MW of 1.7 and 2.3 kDa and also high umami amino acids could be well considered as representative of meaty and umami analog flavors while indicating stronger antioxidant, antihypertension, and antidiabetic attributes.

Keywords: antioxidant, antihypertension, and antidiabetic activities; cross‐linking and sonication; lentil peptides; umami taste development.

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Conflict of interest statement

The authors have declared no conflict of interest.

Figures

FIGURE 1

FIGURE 1

SDS‐PAGE patterns of LPC (control), LPH, LPHC, LPHUS, and LPHUSC. LPC was native lentil protein; LPH was Alcalase–Flavourzyme hydrolysates; LPHC was MTGase cross‐linked LPH; LPHUS was treated LPH with ultrasound; LPHUSC was LPH treated with ultrasound and MTGase.

FIGURE 2

FIGURE 2

GPC analysis of MW distribution of LPC (control) (a), LPH (b), LPHC (c), LPHUS (d), and LPHUSC (e). LPC was native lentil protein; LPH was Alcalase–Flavourzyme hydrolysates; LPHC was MTGase cross‐linked LPH; LPHUS was treated LPH with ultrasound; LPHUSC was LPH treated with ultrasound and MTGase.

FIGURE 3

FIGURE 3

DPPH RSA (a) and ABTS RSA (b) of LPC, sequentially hydrolyzed LPC (LPH), cross‐linked LPH (LPHC), sonicated LPH (LPHUS), and sonicated cross‐linked LPH (LPHUSC). Acid ascorbic was used as positive control. The concentration of protein and hydrolysates were 7 mg/mL while it was 0.01 mg/mL for ascorbic acid.

FIGURE 4

FIGURE 4

ACE inhibition of LPC, hydrolyzed LPC (LPH), cross‐linked LPH (LPHC), sonicated LPH (LPHUS), and sonicated cross‐linked LPH (LPHUSC). The concentration of protein and hydrolysates was 2 mg/mL.

FIGURE 5

FIGURE 5

α‐glucosidase inhibition of LPC, hydrolyzed LPC (LPH), sonicated LPH (LPHUS), and sonicated cross‐linked LPH (LPHUSC). The concentration of protein, hydrolysates, and acarbose was 500 μg/mL.

FIGURE 6

FIGURE 6

α‐amylase inhibition of LPC, hydrolyzed LPC (LPH), sonicated LPH (LPHUS), and sonicated cross‐linked LPH (LPHUSC). The concentration of protein, hydrolysates, and acarbose was 500 μg/mL.

FIGURE 7

FIGURE 7

Umami taste scores of LPC, hydrolyzed LPC (LPH), sonicated LPH (LPHUS), and sonicated cross‐linked LPH (LPHUSC).

See this image and copyright information in PMC

References

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1. Ambigaipalan, P. , Al‐Khalifa, A. S. , & Shahidi, F. (2015). Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using alcalase, flavourzyme and thermolysin. Journal of Functional Foods, 18, 1125–1137. 10.1016/j.jff.2015年01月02日1 - DOI
1. Amini Sarteshnizi, R. , Sahari, M. A. , Ahmadi Gavlighi, H. , Regenstein, J. M. , Nikoo, M. , & Udenigwe, C. C. (2021). Influence of fish protein hydrolysate‐pistachio green hull extract interactions on antioxidant activity and inhibition of α‐glucosidase, α‐amylase, and DPP‐IV enzymes. LWT, 142, 111019. 10.1016/J.LWT.2021.111019 - DOI
1. Arise, R. O. , Idi, J. J. , Mic‐Braimoh, I. M. , Korode, E. , Ahmed, R. N. , & Osemwegie, O. (2019). In vitro Angiotesin‐1‐converting enzyme, α‐amylase and α‐glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate. Heliyon, 5(5), e01634. 10.1016/J.HELIYON.2019.E01634 - DOI - PMC - PubMed
1. Aryee, A. N. A. , & Boye, J. I. (2016). Improving the digestibility of lentil flours and protein isolate and characterization of their enzymatically prepared hydrolysates. International Journal of Food Properties, 19(12), 2649–2665. 10.1080/10942912.2015.1123269 - DOI

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[1] Akillioǧlu, H. G. , & Karakaya, S. (2009). Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species. European Food Research and Technology, 229(6), 915–921. 10.1007/s00217-009-1133-x - DOI

[2] Akillioǧlu, H. G. , & Karakaya, S. (2009). Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species. European Food Research and Technology, 229(6), 915–921. 10.1007/s00217-009-1133-x - DOI

[3] Ambigaipalan, P. , Al‐Khalifa, A. S. , & Shahidi, F. (2015). Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using alcalase, flavourzyme and thermolysin. Journal of Functional Foods, 18, 1125–1137. 10.1016/j.jff.2015年01月02日1 - DOI

[4] Ambigaipalan, P. , Al‐Khalifa, A. S. , & Shahidi, F. (2015). Antioxidant and angiotensin I converting enzyme (ACE) inhibitory activities of date seed protein hydrolysates prepared using alcalase, flavourzyme and thermolysin. Journal of Functional Foods, 18, 1125–1137. 10.1016/j.jff.2015年01月02日1 - DOI

[5] Amini Sarteshnizi, R. , Sahari, M. A. , Ahmadi Gavlighi, H. , Regenstein, J. M. , Nikoo, M. , & Udenigwe, C. C. (2021). Influence of fish protein hydrolysate‐pistachio green hull extract interactions on antioxidant activity and inhibition of α‐glucosidase, α‐amylase, and DPP‐IV enzymes. LWT, 142, 111019. 10.1016/J.LWT.2021.111019 - DOI

[6] Amini Sarteshnizi, R. , Sahari, M. A. , Ahmadi Gavlighi, H. , Regenstein, J. M. , Nikoo, M. , & Udenigwe, C. C. (2021). Influence of fish protein hydrolysate‐pistachio green hull extract interactions on antioxidant activity and inhibition of α‐glucosidase, α‐amylase, and DPP‐IV enzymes. LWT, 142, 111019. 10.1016/J.LWT.2021.111019 - DOI

[7] Arise, R. O. , Idi, J. J. , Mic‐Braimoh, I. M. , Korode, E. , Ahmed, R. N. , & Osemwegie, O. (2019). In vitro Angiotesin‐1‐converting enzyme, α‐amylase and α‐glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate. Heliyon, 5(5), e01634. 10.1016/J.HELIYON.2019.E01634 - DOI - PMC - PubMed

[8] Arise, R. O. , Idi, J. J. , Mic‐Braimoh, I. M. , Korode, E. , Ahmed, R. N. , & Osemwegie, O. (2019). In vitro Angiotesin‐1‐converting enzyme, α‐amylase and α‐glucosidase inhibitory and antioxidant activities of Luffa cylindrical (L.) M. Roem seed protein hydrolysate. Heliyon, 5(5), e01634. 10.1016/J.HELIYON.2019.E01634 - DOI - PMC - PubMed

[9] Aryee, A. N. A. , & Boye, J. I. (2016). Improving the digestibility of lentil flours and protein isolate and characterization of their enzymatically prepared hydrolysates. International Journal of Food Properties, 19(12), 2649–2665. 10.1080/10942912.2015.1123269 - DOI

[10] Aryee, A. N. A. , & Boye, J. I. (2016). Improving the digestibility of lentil flours and protein isolate and characterization of their enzymatically prepared hydrolysates. International Journal of Food Properties, 19(12), 2649–2665. 10.1080/10942912.2015.1123269 - DOI

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Development of lentil peptides with potent antioxidant, antihypertensive, and antidiabetic activities along with umami taste

Affiliations

Development of lentil peptides with potent antioxidant, antihypertensive, and antidiabetic activities along with umami taste

Authors

Affiliations

Abstract

Conflict of interest statement

Figures

References

LinkOut - more resources

Full Text Sources

Miscellaneous