The ACE-inhibitory activity of alcalase, papain and pepsin lupin protein hydrolysates The ACE-inhibitory activity of lupin hydrolysates
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Abstract
Recently, Lupinus angustifolius proteins revealed their high potential to liberate bioactive peptides after hydrolysis. In our study, we examined the release of angiotensin I-converting enzyme inhibitory peptides from extracted lupin proteins after digestion by alcalase, papain, and pepsin. Three enzyme-to-substrate ratios were evaluated with three hydrolysis duration times. First, the degree of hydrolysis was determined using the ortho-phthalaldehyde aldehyde (OPA) method and then, the HPLC-DAD method was applied to measure the ACE-inhibitory activity. According to our results, all hydrolysates possessed ACE inhibitory properties. The calculated IC50 concentrations varied from 0.26 ± 0.59 to 2.19 ± 0.23 μg.ml-1. The peptides with the lowest IC50 values were produced by pepsin (ΔIC50 = 0.33 ± 0.40 μg.ml-1), followed by papain (ΔIC50 = 0.67 ± 0.61 μg.ml-1), and alcalase (ΔIC50 = 1.78 ± 0.92 μg.ml-1). Further research on bioavailability is required to demonstrate the beneficial effects of bioactive peptides on human health, since they have to resist digestive processing pass the intestinal barrier, and reach the bloodstream and intended organs.
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References
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Chauhan V., Kanwar S.S., Hill S. Bioactive peptides: Synthesis, functions and biotechnological applications. In: Biotechnological Production of Bioactive Compounds (M.L. Verma, A.K. Chandel Eds). Elsevier B.V, 2019, pp.107-137, eBook ISBN: 978-0-444-64323-0, https://doi.org/10.1016/B978-0-444-64323-0.00004-7
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Daskaya-Dikmen C., Yucetepe A., Karbancioglu-Guler F., Daskaya H. Ozcelik B. Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants. Nutrients, 2017 9(4): 1-19. https://doi.org/10.3390/nu9040316
Fan H., Liu H., Zhang Y., Zhang S., Liu T., Wang D. Review on plant-derived bioactive peptides: biological activities, mechanism of action and utilizations in food development. Journal of Future Foods, 2(2): 143-159. https://doi.org/10.1016/j.jfutfo.2022.03.003
Garmidolova A., Desseva I., Mihaylova, D., Lante A. Bioactive peptides from lupinus spp. seed proteins-state-of-the-art and perspectives. Applied Sciences, 2022, 12(8): 3766. https://doi.org/10.3390/app12083766
Garmidolova A., Desseva I., Mihaylova D., Fidan H., Terziyska M., Pavlov A. Papain hydrolysates of lupin proteins with antioxidant, antimicrobial, and acetylcholinesterase inhibitory activities, Applied Sciences, 2022, 12(23): 3766. https://doi.org/10.3390/app122312370
Gouda K.G.M., Gowda L.R., Rao A.G.A., Prakash V. Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max). Journal of Agricultural and Food Chemistry, 2006, 54(13): 4568-4573. https://doi.org/10.1021/jf060264q
Hayes M., Tiwari B.K. Bioactive carbohydrates and peptides in foods: An overview of sources, downstream processing steps and associated bioactivities. International Journal of Molecular Sciences, 2015, 16(9): 22485-22508. https://doi.org/10.3390/ijms160922485
He H.L., Liu D., Ma C.B. Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins. Applied Biochemistry and Biotechnology, 2013 169(3): 738-749. https://doi.org/10.1007/s12010-012-0024-y
Hunsakul K., Laokuldilok T., Sakdatorn V., Klangpetch W., Brennan C.S., Utama-ang N. Optimization of enzymatic hydrolysis by alcalase and flavourzyme to enhance the antioxidant properties of jasmine rice bran protein hydrolysate. Scientific Reports, 2022 12(1): 1-10. https://doi.org/10.1038/s41598-022-16821-z
Ismail A. Anuar T., Suffian I.F.., Hamid A.A., Omar, M.N., Mustafa B.E. Angiotensin converting enzyme (ACE) inhibition activity by syzygium polyanthum wight (Walp.) leaves: Mechanism and specificity. Pharmacognosy Journal, 2022, 14(1): 76-84. https://doi.org/10.5530/pj.2022.14.11
Iwaniak A., Minkiewicz P., Darewicz M. Food-originating ACE inhibitors, including antihypertensive peptides, as preventive food components in blood pressure reduction. Comprehensive Reviews in Food Science and Food Safety, 2014, 13(2): 114-134. https://doi.org/10.1111/1541-4337.12051
Jin D., Liu X., Zheng X., Wang X., He L. Preparation of antioxidative corn protein hydrolysates, purification and evaluation of three novel corn antioxidant peptides. Food Chemistry, 2016, 204(1): 427-436. https://doi.org/10.1016/j.foodchem.2016.02.119
Johnson, S.K. Clements J., Villarino C., Blanca J, Coorey R. Chapter 8 - Lupins: Their Unique Nutritional and Health-Promoting Attributes. In: Gluten-Free Ancient Grains. Cereals, Pseudocereals, and Legumes: Sustainable, Nutritious, and Health-Promoting Foods for the 21st Century (J.R.N. Taylor, J.M. Awika Eds). Woodhead Publishing Series in Food Science, Technology and Nutrition. Elsevier Ltd. 2017, pp. 179-221. Print ISBN: 978-0-08-100866-9 https://doi.org/10.1016/B978-0-08-100866-9.00008-X
Kamran F. Enzymatic Hydrolysis of Lupin (Lupinus angustifolius) Protein: Isolation and Characterization of Bioactive Peptides. PhD thesis by Western Sydney University, 2017 [in English]
Lambers H., Clements J.C., Nelson M.N. How aphosphorus-acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae). American Journal of Botany, 2013, 100(2): 263-288. https://doi.org/10.3732/ajb.1200474
Lee S.Y., Hur S.J. Antihypertensive peptides from animal products, marine organisms, and plants. Food Chemistry, 2017, 228(2): 506-517. https://doi.org/10.1016/j.foodchem.2017.02.039
de Leo F., Panarese S., Gallerani R., Ceci L. Angiotensin converting enzyme (ACE) inhibitory peptides: Production and implementation of functional food. Current Pharmaceutical Design, 2009, 15(31): 3622-3643. https://doi.org/10.2174/138161209789271834
Lo B., Kasapis S., Farahnaky A. Lupin protein: Isolation and techno-functional properties, a review. Food Hydrocolloids, 2021, 112(3): 106318. https://doi.org/10.1016/j.foodhyd.2020.106318
Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. The Journal of Biological Chemistry, 1951, 193(1): 265-275. https://doi.org/10.1016/s0021-9258(19)52451-6
F.F. Ma H., Wang C.K., Wei K. Thakur Z.J., Wei J. Three novel ACE inhibitory peptides isolated from ginkgo biloba seeds: Purification, inhibitory kinetic and mechanism. Frontiers in Pharmacology, 2019, 9(1): 1579. https://doi.org/10.3389/fphar.2018.01579
Mat Amin A.B. Optimization of enzymatic protein hydrolysis conditions to obtain maximum angiotensin-iconverting enzyme (ACE) inhibitory activity from angel wing clam (Pholas orientalis) meat. Madridge Journal of Food Technology, 2017 2(1): 65-73. https://doi.org/10.18689/mjft-1000110
Mehanna A.S., Dowling M. Liquid chromatographic determination of hippuric acid for the evaluation of ethacrynic acid as angiotensin converting enzyme inhibitor. Journal of Pharmaceutical and Biomedical Analysis, 1999. 19(6): 967-973. https://doi.org/10.1016/S0731-7085(98)00122-8
Minervini F., Algaron F., Rizzello C.G., Fox P.F., Monnet V., Gobbetti M. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology, 2003, 69(9): 5297-5305. https://doi.org/10.1128/AEM.69.9.5297-5305.2003
Mirzapour-Kouhdasht A., Garcia-vaquero M., Eun J. Fractionation on the antioxidant and lipase/α-mylase inhibitory activities in vitro of watermelon seed protein hydrolysates. Molecules, 2022, 27(22): 7897. https://doi.org/10.3390/molecules27227897
Motoi H., Kodama T. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate. Molecular Nutrition & Food Research, 2003, 47(5): 354-358. https://doi.org/10.1002/FOOD.200390081
Murray B., FitzGerald R. Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design, 2007, 13(8): 773-791. https://doi.org/10.2174/138161207780363068
Muthia R., Suganda A.G., Sukandar E.Y. Angiotensin-I converting enzyme (ACE) inhibitory activity of several Indonesian medicinal plants. Research Journal of Pharmaceutical, Biological and Chemical Sciences, 2017, 8(1S): 192-199. Available at: https://www.rjpbcs.com/pdf/2017_8(1S)/[29].pdf
Nielsen P.M., Petersen D., Dambmann C. Improved method for determining food protein degree of hydrolysis. Journal of Food Science, 2001, 66(5): 642-646. https://doi.org/10.1111/j.1365-2621.2001.tb04614.x
Okagu, I.U., Ndefo J., Aha E., Obeme-Nmom J., Agboinghale E., Aguchem R., Nechi R., Lammi C. Lupin-derived bioactive peptides: Intestinal transport, bioavailability and health benefits. Nutrients, 2021, 13(9): 3266. https://doi.org/10.3390/nu13093266
Paiva L., Lima E., Neto A., Baptista J. Angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant properties, phenolic content and amino acid profiles of Fucus spiralis L. protein hydrolysate fractions. Marine Drugs, 2017, 15(10): 311. https://doi.org/10.3390/md15100311
Pinto M., Silva, Mauro R., Silva V., Souza M., Lopes C., Afonso W. Analysis of whey protein hydrolysates: peptide profile and ACE inhibitory activity. Brazilian Journal of Pharmaceutical Sciences, 2012, 48(4): 747-757. https://doi.org/10.1590/S1984-82502012000400019
Rizzello C.G. Bioactive peptides from vegetable food matrices: Research trends and novel biotechnologies for synthesis and recovery. Journal of Functional Foods, 27(12): 549-569. https://doi.org/10.1016/j.jff.2016.09.023
Roberts P.R., Burney J.D, Black K.W., Zaloga G.P. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion, 1999, 60(4): 332-337. https://doi.org/10.1159/000007679
Sbroggio M.F., Montilha M.S., Ribeiro V., Figueiredo G.De, Georgetti S.R., Kurozawa L.E. Influence of the degree of hydrolysis and type of enzyme on antioxidant activity of okara protein hydrolysates. Food Science and Technology [Ciência e Tecnologia de Alimentos], 2016, 36(2): 375-381. https://doi.org/10.1590/1678-457X.000216
Shahidi F., Zhong Y. Bioactive peptides. Journal of AOAC International, 2008, 91(4): 914-931. https://doi.org/10.1093/jaoac/91.4.914
Sipsas S. Lupin Products - Concepts and Reality. 12th International Lupin Conference, Western Australia, 2008, pp. 506-513. Available at: https://www.scribd.com/document/330736246/LUPIN-PRODUCTS-CONCEPTS-AND-REALITY-pdf
Tawalbeh D., Al-U’datt M., Wan Ahmad W., Ahmad F., Sarbon M. ACE-Inhibitory and anti-inflammatory peptides from legume protein hydrolysates. Molecules, 2023, 28(6): 2423. https://doi.org/10.3390/molecules28062423
Udenigwe C.C. Mechanisms of food protein-derived antihypertensive peptides other than ACE inhibition. Journal of Functional Foods, 2014 8(5): 45-52. https://doi.org/10.1016/j.jff.2014.03.002
Vermeirssen V., Camp J. Van and Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. British Journal of Nutrition, 2004, 92(3): 357-366. https://doi.org/10.1079/bjn20041189
Vogelsang-O’Dwyer M., Bez J.,Petersen I., Joehnke M., Detzel A., Busch M., Krueger M., Ispiryan L., O’Mahony J., Arendt E. Techno-functional, nutritional and environmental performance of protein isolates from blue lupin and white lupin. Foods, 2020, 9(2): 230. https://doi.org/10.3390/foods9020230
Zaky A.A., Simal-Gandara J., Eun J.B., Shim J.H., Abd El-Aty A.M. Bioactivities, applications, safety, and health benefits of bioactive peptides from food and by-products: A review. Frontiers in Nutrition, 2022, 8(1): 815640. https://doi.org/10.3389/fnut.2021.815640
Boschin G., Scigliuolo G.M., Resta M., Arnoldi A. Optimization of the enzymatic hydrolysis of lupin (Lupinus) proteins for producing ACE-inhibitory peptides. Journal of Agricultural and Food Chemistry, 2014, 62(8): 1846-1851. https://doi.org/10.1021/jf4039056
Chauhan V., Kanwar S.S., Hill S. Bioactive peptides: Synthesis, functions and biotechnological applications. In: Biotechnological Production of Bioactive Compounds (M.L. Verma, A.K. Chandel Eds). Elsevier B.V, 2019, pp.107-137, eBook ISBN: 978-0-444-64323-0, https://doi.org/10.1016/B978-0-444-64323-0.00004-7
Daliri E.B.M., Lee B.H., Oh D.H. Current trends and perspectives of bioactive peptides. Critical Reviews in Food Science and Nutrition, 58(13): 2273-2284. https://doi.org/10.1080/10408398.2017.1319795
Daskaya-Dikmen C., Yucetepe A., Karbancioglu-Guler F., Daskaya H. Ozcelik B. Angiotensin-I-converting enzyme (ACE)-inhibitory peptides from plants. Nutrients, 2017 9(4): 1-19. https://doi.org/10.3390/nu9040316
Fan H., Liu H., Zhang Y., Zhang S., Liu T., Wang D. Review on plant-derived bioactive peptides: biological activities, mechanism of action and utilizations in food development. Journal of Future Foods, 2(2): 143-159. https://doi.org/10.1016/j.jfutfo.2022.03.003
Garmidolova A., Desseva I., Mihaylova, D., Lante A. Bioactive peptides from lupinus spp. seed proteins-state-of-the-art and perspectives. Applied Sciences, 2022, 12(8): 3766. https://doi.org/10.3390/app12083766
Garmidolova A., Desseva I., Mihaylova D., Fidan H., Terziyska M., Pavlov A. Papain hydrolysates of lupin proteins with antioxidant, antimicrobial, and acetylcholinesterase inhibitory activities, Applied Sciences, 2022, 12(23): 3766. https://doi.org/10.3390/app122312370
Gouda K.G.M., Gowda L.R., Rao A.G.A., Prakash V. Angiotensin I-converting enzyme inhibitory peptide derived from glycinin, the 11S globulin of soybean (Glycine max). Journal of Agricultural and Food Chemistry, 2006, 54(13): 4568-4573. https://doi.org/10.1021/jf060264q
Hayes M., Tiwari B.K. Bioactive carbohydrates and peptides in foods: An overview of sources, downstream processing steps and associated bioactivities. International Journal of Molecular Sciences, 2015, 16(9): 22485-22508. https://doi.org/10.3390/ijms160922485
He H.L., Liu D., Ma C.B. Review on the angiotensin-I-converting enzyme (ACE) inhibitor peptides from marine proteins. Applied Biochemistry and Biotechnology, 2013 169(3): 738-749. https://doi.org/10.1007/s12010-012-0024-y
Hunsakul K., Laokuldilok T., Sakdatorn V., Klangpetch W., Brennan C.S., Utama-ang N. Optimization of enzymatic hydrolysis by alcalase and flavourzyme to enhance the antioxidant properties of jasmine rice bran protein hydrolysate. Scientific Reports, 2022 12(1): 1-10. https://doi.org/10.1038/s41598-022-16821-z
Ismail A. Anuar T., Suffian I.F.., Hamid A.A., Omar, M.N., Mustafa B.E. Angiotensin converting enzyme (ACE) inhibition activity by syzygium polyanthum wight (Walp.) leaves: Mechanism and specificity. Pharmacognosy Journal, 2022, 14(1): 76-84. https://doi.org/10.5530/pj.2022.14.11
Iwaniak A., Minkiewicz P., Darewicz M. Food-originating ACE inhibitors, including antihypertensive peptides, as preventive food components in blood pressure reduction. Comprehensive Reviews in Food Science and Food Safety, 2014, 13(2): 114-134. https://doi.org/10.1111/1541-4337.12051
Jin D., Liu X., Zheng X., Wang X., He L. Preparation of antioxidative corn protein hydrolysates, purification and evaluation of three novel corn antioxidant peptides. Food Chemistry, 2016, 204(1): 427-436. https://doi.org/10.1016/j.foodchem.2016.02.119
Johnson, S.K. Clements J., Villarino C., Blanca J, Coorey R. Chapter 8 - Lupins: Their Unique Nutritional and Health-Promoting Attributes. In: Gluten-Free Ancient Grains. Cereals, Pseudocereals, and Legumes: Sustainable, Nutritious, and Health-Promoting Foods for the 21st Century (J.R.N. Taylor, J.M. Awika Eds). Woodhead Publishing Series in Food Science, Technology and Nutrition. Elsevier Ltd. 2017, pp. 179-221. Print ISBN: 978-0-08-100866-9 https://doi.org/10.1016/B978-0-08-100866-9.00008-X
Kamran F. Enzymatic Hydrolysis of Lupin (Lupinus angustifolius) Protein: Isolation and Characterization of Bioactive Peptides. PhD thesis by Western Sydney University, 2017 [in English]
Lambers H., Clements J.C., Nelson M.N. How aphosphorus-acquisition strategy based on carboxylate exudation powers the success and agronomic potential of lupines (Lupinus, Fabaceae). American Journal of Botany, 2013, 100(2): 263-288. https://doi.org/10.3732/ajb.1200474
Lee S.Y., Hur S.J. Antihypertensive peptides from animal products, marine organisms, and plants. Food Chemistry, 2017, 228(2): 506-517. https://doi.org/10.1016/j.foodchem.2017.02.039
de Leo F., Panarese S., Gallerani R., Ceci L. Angiotensin converting enzyme (ACE) inhibitory peptides: Production and implementation of functional food. Current Pharmaceutical Design, 2009, 15(31): 3622-3643. https://doi.org/10.2174/138161209789271834
Lo B., Kasapis S., Farahnaky A. Lupin protein: Isolation and techno-functional properties, a review. Food Hydrocolloids, 2021, 112(3): 106318. https://doi.org/10.1016/j.foodhyd.2020.106318
Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the Folin phenol reagent. The Journal of Biological Chemistry, 1951, 193(1): 265-275. https://doi.org/10.1016/s0021-9258(19)52451-6
F.F. Ma H., Wang C.K., Wei K. Thakur Z.J., Wei J. Three novel ACE inhibitory peptides isolated from ginkgo biloba seeds: Purification, inhibitory kinetic and mechanism. Frontiers in Pharmacology, 2019, 9(1): 1579. https://doi.org/10.3389/fphar.2018.01579
Mat Amin A.B. Optimization of enzymatic protein hydrolysis conditions to obtain maximum angiotensin-iconverting enzyme (ACE) inhibitory activity from angel wing clam (Pholas orientalis) meat. Madridge Journal of Food Technology, 2017 2(1): 65-73. https://doi.org/10.18689/mjft-1000110
Mehanna A.S., Dowling M. Liquid chromatographic determination of hippuric acid for the evaluation of ethacrynic acid as angiotensin converting enzyme inhibitor. Journal of Pharmaceutical and Biomedical Analysis, 1999. 19(6): 967-973. https://doi.org/10.1016/S0731-7085(98)00122-8
Minervini F., Algaron F., Rizzello C.G., Fox P.F., Monnet V., Gobbetti M. Angiotensin I-converting-enzyme-inhibitory and antibacterial peptides from Lactobacillus helveticus PR4 proteinase-hydrolyzed caseins of milk from six species. Applied and Environmental Microbiology, 2003, 69(9): 5297-5305. https://doi.org/10.1128/AEM.69.9.5297-5305.2003
Mirzapour-Kouhdasht A., Garcia-vaquero M., Eun J. Fractionation on the antioxidant and lipase/α-mylase inhibitory activities in vitro of watermelon seed protein hydrolysates. Molecules, 2022, 27(22): 7897. https://doi.org/10.3390/molecules27227897
Motoi H., Kodama T. Isolation and characterization of angiotensin I-converting enzyme inhibitory peptides from wheat gliadin hydrolysate. Molecular Nutrition & Food Research, 2003, 47(5): 354-358. https://doi.org/10.1002/FOOD.200390081
Murray B., FitzGerald R. Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design, 2007, 13(8): 773-791. https://doi.org/10.2174/138161207780363068
Muthia R., Suganda A.G., Sukandar E.Y. Angiotensin-I converting enzyme (ACE) inhibitory activity of several Indonesian medicinal plants. Research Journal of Pharmaceutical, Biological and Chemical Sciences, 2017, 8(1S): 192-199. Available at: https://www.rjpbcs.com/pdf/2017_8(1S)/[29].pdf
Nielsen P.M., Petersen D., Dambmann C. Improved method for determining food protein degree of hydrolysis. Journal of Food Science, 2001, 66(5): 642-646. https://doi.org/10.1111/j.1365-2621.2001.tb04614.x
Okagu, I.U., Ndefo J., Aha E., Obeme-Nmom J., Agboinghale E., Aguchem R., Nechi R., Lammi C. Lupin-derived bioactive peptides: Intestinal transport, bioavailability and health benefits. Nutrients, 2021, 13(9): 3266. https://doi.org/10.3390/nu13093266
Paiva L., Lima E., Neto A., Baptista J. Angiotensin I-converting enzyme (ACE) inhibitory activity, antioxidant properties, phenolic content and amino acid profiles of Fucus spiralis L. protein hydrolysate fractions. Marine Drugs, 2017, 15(10): 311. https://doi.org/10.3390/md15100311
Pinto M., Silva, Mauro R., Silva V., Souza M., Lopes C., Afonso W. Analysis of whey protein hydrolysates: peptide profile and ACE inhibitory activity. Brazilian Journal of Pharmaceutical Sciences, 2012, 48(4): 747-757. https://doi.org/10.1590/S1984-82502012000400019
Rizzello C.G. Bioactive peptides from vegetable food matrices: Research trends and novel biotechnologies for synthesis and recovery. Journal of Functional Foods, 27(12): 549-569. https://doi.org/10.1016/j.jff.2016.09.023
Roberts P.R., Burney J.D, Black K.W., Zaloga G.P. Effect of chain length on absorption of biologically active peptides from the gastrointestinal tract. Digestion, 1999, 60(4): 332-337. https://doi.org/10.1159/000007679
Sbroggio M.F., Montilha M.S., Ribeiro V., Figueiredo G.De, Georgetti S.R., Kurozawa L.E. Influence of the degree of hydrolysis and type of enzyme on antioxidant activity of okara protein hydrolysates. Food Science and Technology [Ciência e Tecnologia de Alimentos], 2016, 36(2): 375-381. https://doi.org/10.1590/1678-457X.000216
Shahidi F., Zhong Y. Bioactive peptides. Journal of AOAC International, 2008, 91(4): 914-931. https://doi.org/10.1093/jaoac/91.4.914
Sipsas S. Lupin Products - Concepts and Reality. 12th International Lupin Conference, Western Australia, 2008, pp. 506-513. Available at: https://www.scribd.com/document/330736246/LUPIN-PRODUCTS-CONCEPTS-AND-REALITY-pdf
Tawalbeh D., Al-U’datt M., Wan Ahmad W., Ahmad F., Sarbon M. ACE-Inhibitory and anti-inflammatory peptides from legume protein hydrolysates. Molecules, 2023, 28(6): 2423. https://doi.org/10.3390/molecules28062423
Udenigwe C.C. Mechanisms of food protein-derived antihypertensive peptides other than ACE inhibition. Journal of Functional Foods, 2014 8(5): 45-52. https://doi.org/10.1016/j.jff.2014.03.002
Vermeirssen V., Camp J. Van and Verstraete W. Bioavailability of angiotensin I converting enzyme inhibitory peptides. British Journal of Nutrition, 2004, 92(3): 357-366. https://doi.org/10.1079/bjn20041189
Vogelsang-O’Dwyer M., Bez J.,Petersen I., Joehnke M., Detzel A., Busch M., Krueger M., Ispiryan L., O’Mahony J., Arendt E. Techno-functional, nutritional and environmental performance of protein isolates from blue lupin and white lupin. Foods, 2020, 9(2): 230. https://doi.org/10.3390/foods9020230
Zaky A.A., Simal-Gandara J., Eun J.B., Shim J.H., Abd El-Aty A.M. Bioactivities, applications, safety, and health benefits of bioactive peptides from food and by-products: A review. Frontiers in Nutrition, 2022, 8(1): 815640. https://doi.org/10.3389/fnut.2021.815640
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How to Cite
GARMIDOLOVA, Aleksandra Stefanova; DESSEVA, Ivelina.
The ACE-inhibitory activity of alcalase, papain and pepsin lupin protein hydrolysates.
Food Science and Applied Biotechnology, [S.l.], v. 6, n. 2, p. 395-404, oct. 2023.
ISSN 2603-3380.
Available at: <https://www.ijfsab.com/index.php/fsab/article/view/287>. Date accessed: 12 sep. 2024.
doi: https://doi.org/10.30721/fsab2023.v6.i2.287.