Plant Foods for Human Nutrition

, Volume 71, Issue 3, pp 339–345 | Cite as

Bioactive Properties of Phaseolus lunatus (Lima Bean) and Vigna unguiculata (Cowpea) Hydrolyzates Incorporated into Pasta. Residual Activity after Pasta Cooking

  • Silvina R. Drago
  • Hanai Franco-Miranda
  • Raúl E. Cian
  • David Betancur-Ancona
  • Luis Chel-GuerreroEmail author
Original Paper


The aims of the study were to study the inclusion of P. lunatus (PLH) and V. unguiculata (VUH) protein hydrolyzates with bioactive properties into a pasta-extruded product and determine residual activity after extrusion or pasta cooking. Both protein hydrolyzates showed angiotensin-converting enzyme inhibition (ACEI) and antioxidant activity (TEAC). PLH showed higher ACEI but lower TEAC than VUH (97.19 ± 0.23 vs. 91.95 ± 0.29 % and 244.7 ± 3.4 vs. 293.7 ± 3.3 μmol Trolox/g, respectively). They were included at 5 or 10 % into wheat pasta. Control pasta had the lowest ACEI activity or TEAC (22.01 ± 0.76 % or 14.14 ± 1.28 μmol Trolox/g, respectively). Higher activity remained in pasta with PLH than VUH after extrusion, and higher the level of addition, higher the ACEI was. Pasta had practically the same ACEI activity after cooking, thus active compounds were not lost by temperature or lixiviation. Regarding TEAC, higher activity remained in pasta with 10 % VUH (31.84 ± 0.17 μmol Trolox/g). Other samples with hydrolyzates had the same activity. After cooking, pasta with hydrolyzates had higher TEAC values than control, but these were not modified by the level of incorporation. Moreover, the profile changed because pasta with PLH had the highest TEAC values (21.39 ± 0.01 and 20.34 ± 0.15 for 5 or 10 % hydrolyzates, respectively). Cooking decreased this activity (~ 20 %), for all samples. Although a certain loss of antioxidant activity was observed, pasta could be a good vehicle for bioactive compounds becoming a functional food.


Lima bean Cowpea Functional foods Antihypertensive Antioxidant activity 



Phaseolus lunatus hydrolyzate


Vigna unguiculata hydrolyzate


Angiotensin-converting enzyme inhibition activity


Trolox equivalent antioxidant capacity


Protein concentrate


Phaseolus lunatus protein concentrate


Vigna unguiculata protein concéntrate


Nitrogen-free extract


Dry base



This research was supported by CONACYT and PROMEP-SEP-México.

Compliance with Ethical Standards

Conflict of Interest

The authors declare no conflicts of interest.

Human and Animals Studies

This article does not contain any studies with human or animal subjects.


  1. 1.
    Chel-Guerrero L, Domínguez-Magaña M, Martínez-Ayala A, Dávila-Ortiz G, Betancur-Ancona D (2012) Lima bean (Phaseolus lunatus) protein hydrolysates with ACE-I inhibitory activity. Food Nutr Sci 3:511–521CrossRefGoogle Scholar
  2. 2.
    Segura-Campos MR, García-Espinosa L, Chel-Guerrero L, Betancur-Ancona D (2012) Effect of enzymatic hydrolysis on solubility, hydrophobicity, and in vivo digestibility in cowpea (Vigna unguiculata). Int J Food Prop 15:770–780CrossRefGoogle Scholar
  3. 3.
    Doucet D, Otter DE, Gauthier SF, Foegeding EA (2003) Enzyme induced gelation of extensively hydrolyzed whey proteins by alcalase: peptide identification and determination of enzyme specificity. J Agric Food Chem 51:6300–6308CrossRefGoogle Scholar
  4. 4.
    Cian R, Vioque J, Drago S (2015) Structure–mechanism relationship of antioxidant and ACE I inhibitory peptides from wheat gluten hydrolysate fractionated by pH. Food Res Int 69:216–223CrossRefGoogle Scholar
  5. 5.
    Cian R, Garzón A, Betancur Ancona D, Chel Guerrero L, Drago S (2016) Chelating properties of peptides from red seaweed Pyropia columbina and its effect on iron bio-accessibility. Plant Foods Hum Nutr 71:96–101CrossRefGoogle Scholar
  6. 6.
    Young V, Pellett P (1994) Plant proteins in relation to human protein and amino acid nutrition. Am J Clin Nutr 59:1203S–1212SGoogle Scholar
  7. 7.
    Giménez A, Drago SR, Bassett MN, Lobo MO, Sammán NC (2016) Nutritional improvement of corn pasta-like product with broad bean (Vicia faba) and quinoa (Chenopodium quinoa). Food Chem 199:150–156CrossRefGoogle Scholar
  8. 8.
    Segura-Campos M, García-Rodríguez K, Ruiz-Ruiz J, Chel-Guerrero L, Betancur-Ancona D (2014) In vitro bioactivity, nutritional and sensory properties of semolina pasta added with hard-to-cook bean (Phaseolus vulgaris) protein hydrolyzate. J Funct Foods 8:1–8CrossRefGoogle Scholar
  9. 9.
    Guzmán-Méndez B, Jaramillo-Flores M, Chel-Guerrero L, Betancur-Ancona D (2014) Comparison of physicochemical properties, antioxidant and metal-chelating activities of protein hydrolysates from Phaseolus lunatus and hard-to-cook Phaseolus vulgaris. Int J Food Sci Technol 49:1–10CrossRefGoogle Scholar
  10. 10.
    Betancur-Ancona D, Peraza-Mercado G, Moguel-Ordoñez Y, Fuertes-Blanco S (2004) Physicochemical characterization of lima bean (Phaseolus lunatus) and Jack bean (Canavalia ensiformis) fibrous residues. Food Chem 84:287–295CrossRefGoogle Scholar
  11. 11.
    Megías C, Yust MM, Pedroche J, Lquarit T, Giron-Calle J, Alaíz M, Millan F, Vioque J (2004) Purification of an ACE inhibitory peptide alter hydrolysis of sunflower (Helianthus annnus L.) protein isolates. J Agric Food Chem 52:1928–1932CrossRefGoogle Scholar
  12. 12.
    Nielsen PM, Peterson D, Dambmann C (2001) Improved method for determining food protein degree of hydrolysis. J Food Sci 66:642–646CrossRefGoogle Scholar
  13. 13.
    AOAC (1997) Official methods of analysis. Association of Official Analytical Chemists. 17th ed. Washington, D.C. USA, William Howitz Editor, 1110–1117Google Scholar
  14. 14.
    Hayakari M, Kondo Y, Izumi H (1978) A rapid and simple spectrophotometric assay of angiotensin-converting enzyme. Anal Biochem 84:361–369CrossRefGoogle Scholar
  15. 15.
    Cian R, Luggren P, Drago SR (2011) Effect of extrusion process on antioxidant and ACE inhibition properties from bovine haemoglobin concentrate hydrolyzates incorporated into expanded maize products. Int J Food Sci Nutr 62:774–780CrossRefGoogle Scholar
  16. 16.
    Del Nobile MA, Baianao A, Mocci G (2005) Influence of protein content on spaghetti cooking quality. J Cereal Sci 41:347–356CrossRefGoogle Scholar
  17. 17.
    Siddhuraju P, Vijayakumari K, Janaradhanan K (1994) Chemical analysis and nutritional assessment of the less known pulses, Vigna aconitifolia (Jacq.) Marechal and Vigna vexillata (L.) a. Rich. Plant Foods Hum Nutr 45:103–111CrossRefGoogle Scholar
  18. 18.
    Barać M, Čabrilo S, Pešić M, Stanojević S, Pavlićević M, Maćej O, Ristić N (2011) Functional properties of pea (Pisum sativum, L.) protein isolates modified with Chymosin. Int J Mol Sci 12:8372–8387CrossRefGoogle Scholar
  19. 19.
    Gallegos-Infante JA, García-Rivas M, Chang S, Manthey F, Fang R, Reynoso-Camacho R, Rocha-Guzmán NE, González-Laredo RF (2012) Effect of the addition of common bean flour on the cooking quality and antioxidant characteristics of spaghetti. J Microbiol Biotechnol Food Sci 2:730–744. Google Scholar
  20. 20.
    Gallegos-Infante JA, Rocha-Guzman NE, González-Laredo RF, Ochoa LA, Corzo N, Bello LA, Medina L, Peralta-Alvarez LE (2010) Quality of spaghetti pasta containing Mexican common bean flour (Phaseolus vulgaris, L.). J Food Chem 119:1544–1549CrossRefGoogle Scholar
  21. 21.
    Giménez MA, Drago SR, De Greef D, González RJ, Lobo MO, Samman NC (2012) Rheological, functional and nutritional properties of wheat/broad bean (Vicia faba) flour blends for pasta formulation. Food Chem 134:200–206CrossRefGoogle Scholar
  22. 22.
    Petitot M, Boyer L, Minier C, Micard V (2010) Fortification of pasta with split pea and faba beans flours: pasta processing and quality evaluation. Food Res Int 43:634–641CrossRefGoogle Scholar
  23. 23.
    Zhao H, Manthey A, Chang R, Hou H, Yuan H (2005) Quality characteristic of spaghetti as effect by green and yellow pea, lentil and chickpea flours. J Food Sci 70:371–380CrossRefGoogle Scholar
  24. 24.
    Carini E, Vittadini E, Curti E, Antozzani F, Viazzani P (2010) Effect of different mixers on physicochemical properties and water status of extruded and laminated fresh pasta. J Food Chem 122:462–469CrossRefGoogle Scholar
  25. 25.
    Doxastakis G, Papogeorgiou M, Mandalo D, Irakli M, Papalmprou E, D’Agostina A, Resta D, Boschin G, Arnoldi A (2007) Technological properties and non-enzimatic browning of white lupin protein eriched spaghetti. J Food Chem 101:57–64CrossRefGoogle Scholar
  26. 26.
    Segura-Campos MR, Salazar-Vega IM, Chel-Guerrero LA, Betancur-Ancona DA (2013) Biological potential of chia (Salvia hispanica L.) protein hydrolyzates and their incorporation into functional foods. LWT Food Sci Technol 50:723–731CrossRefGoogle Scholar
  27. 27.
    Cian RE, Caballero MS, Sabbag N, González RJ, Drago SR (2014) Bio-accessibility of bioactive compounds (ACE inhibitors and antioxidants) from extruded maize products added with a red seaweed Porphyra columbina. LWT Food Sci Technol 55:51–5Google Scholar
  28. 28.
    Kim S, Wijesekara I (2010) Development and biological activities of marine derived bioactive peptides: a review. J Funct Foods 2:1–9CrossRefGoogle Scholar
  29. 29.
    Dávalos A, Miguel M, Bartolomé B, López-Fadiño R (2004) Antioxidant activity of peptides derived from egg white proteins by enzymatic hydrolysis. J Food Prot 67:1939–1944Google Scholar

Copyright information

© Springer Science+Business Media New York 2016

Authors and Affiliations

  • Silvina R. Drago
    • 1
  • Hanai Franco-Miranda
    • 2
  • Raúl E. Cian
    • 1
  • David Betancur-Ancona
    • 2
  • Luis Chel-Guerrero
    • 2
    Email author
  1. 1.Instituto de Tecnología de AlimentosCONICET, FIQ – UNLSanta FeRepública Argentina
  2. 2.Facultad de Ingeniería QuímicaUniversidad Autónoma de YucatánMéridaMéxico

Personalised recommendations