Angiotensin-converting enzyme-inhibitory activity in protein hydrolysates from normal and anthracnose disease-damaged Phaseolus vulgaris seeds

Journal of the Science of Food and Agriculture

Volumn 93, Issue 4, 2013, Pages 961-966

  Hernández Álvarez, Alan Javier ^a   Carrasco Castilla, Janet ^a   Dávila Ortiz, Gloria ^a   Alaiz, Manuel ^b   Girón Calle, Julio ^b   Vioque Peña, Javier ^b   Jacinto Hernández, Carmen ^c   Jiménez Martínez, Cristian ^a  

^a INSTITUTO POLITÉCNICO NACIONAL   (Mexico)

^b INSTITUTO DE LA GRASA   (Spain)

^c INSTITUTO NACIONAL DE INVESTIGACIONES FORESTALES   (Mexico)

Author keywords

ACE I inhibitory peptides; Anthracnose disease; Bioactive peptides; Phaseolus vulgaris; Protein hydrolysates

Indexed keywords

DIPEPTIDYL CARBOXYPEPTIDASE; DIPEPTIDYL CARBOXYPEPTIDASE INHIBITOR; PEPTIDE; PROTEIN HYDROLYSATE; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; FUNGUS; HYDROLYSIS; IC 50; METABOLISM; MICROBIOLOGY; PHASEOLUS; PLANT DISEASE; PLANT SEED;

ANGIOTENSIN-CONVERTING ENZYME INHIBITORS; FUNGI; HYDROLYSIS; INHIBITORY CONCENTRATION 50; PEPTIDES; PEPTIDYL-DIPEPTIDASE A; PHASEOLUS; PLANT DISEASES; PLANT PROTEINS; PROTEIN HYDROLYSATES; SEEDS;

FUNGI; GLOMERELLA LINDEMUTHIANA; PHASEOLUS VULGARIS;

EID: 84874022781     PISSN: 00225142     EISSN: 10970010     Source Type: Journal    
DOI: 10.1002/jsfa.5841     Document Type: Article

References (37)

1. Smacchi E and Gobbetti M, Bioactive peptides in dairy products: synthesis and interaction with proteolytic enzymes. Food Microbiol 17: 129-141 (2000).
2. Vioque J, Clemente A, Pedroche J, Yust MM and Millán F, Obtention and uses of protein hydrolysates. Grasas y Aceites 52: 132-136 (2001).
3. Frokjaer S, Use of hydrolysates for protein supplementation. Food Technol 48: 86-88 (1994).
4. Pedroche J, Yust MM, Girón-Calle J, Alaiz M, Millán F and Vioque J, Utilisation of chickpea protein isolates for production of peptides with angiotensin I-converting enzyme (ACE)-inhibitory activity. J Sci Food Agric 82: 960-965 (2002).
5. Kim SK, Byun HG, Park PJ and Shahidi F, Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate. J Agric Food Chem 49: 2992-2997 (2001).
6. Swindell WR, Huebner M and Weber AP, Transcriptional profiling of Arabidopsis heat shock proteins and transcription factors reveals extensive overlap between heat and non-heat stress response pathways. BMC Genomics 8(1): 125 (2007).
7. Wang W, Vinocur B, Shoseyov O and Altman A, Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response. Trends Plant Sci 9: 244-252 (2004).
8. González M, Rodríguez R, Zavala ME, Jacobo JL, Hernández F, Acosta J, et al, Characterization of Mexican isolates of Colletotrichum lindemuthianum by using differential cultivars and molecular markers. Phytopathology 88: 292-299 (1998).
9. Pastor-Corrales MA, Otoya MM, Molina A and Singh SP, Resistance to Colletotrichum lindemuthianum isolates from Middle America and Andean South America in different common bean races. Plant Dis 79: 63-67 (1995).
10. Pynenburg GM, Sikkema PH and Gillard CL, Agronomic and economic assessment of intensive pest management of dry bean (Phaseolus vulgaris). Crop Protect 30: 340-348 (2011).
11. Trutmann P, Paul KB and Cishabayo D, Seed treatments increase yield of farmer varietal field bean mixtures in the central African highlands through multiple disease and beanfly control. Crop Protect 11: 458-464 (1992).
12. Timperio AM, Egidi MG and Zolla L, Proteomics applied on plant abiotic stresses: role of heat shock proteins (HSP). J Proteom 71: 391-411 (2008).
13. Torruco-Uco J, Chel-Guerrero L, Martínez-Ayala A, Dávila-Ortíz G and Betancur-Ancona D, Angiotensin-I converting enzyme inhibitory and antioxidant activities of protein hydrolysates from Phaseolus lunatus and Phaseolus vulgaris seeds. LWT-Food Sci Technol 42: 1597-1604 (2009).
14. Akillioǧlu HG and Karakaya S, Effects of heat treatment and in vitro digestion on the angiotensin converting enzyme inhibitory activity of some legume species. Eur Food Res Technol 229: 915-921 (2009).
15. Ruiz-Ruiz J, Dávila-Ortíz G, Chel-Guerrero L and Betancur-Ancona D, Angiotensin I-converting enzyme inhibitory and antioxidant peptide fractions from hard-to-cook bean enzymatic hydrolysates. J Food Biochem in press (2012).
16. Valdez-Ortiz A, Fuentes-Gutiérrez CI, Germán-Báez LJ, Gutiérrez-Dorado R and Medina-Godoy S, Protein hydrolysates obtained from Azufrado (sulphur yellow) beans (Phaseolus vulgaris): nutritional, ACE-inhibitory and antioxidative characterization. LWT-Food Sci Technol 46: 91-96 (2012).
17. AOAC, Official Methods of Analysis (16th edn). Association of Official Analytical Chemists, Arlington, VA (1995).
18. Kim SY, Park PSW and Rhee KC, Functional properties of proteolytic enzyme modified soy protein isolate. J Agric Food Chem 38: 651-656 (1990).
19. Hayakari M, Kondo Y and Izumi H, A rapid and simple spectrophotometric assay of angiotensin-converting enzyme. Anal Biochem 84: 361-369 (1978).
20. Laemmli UK, Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685 (1970).
21. Alaiz M, Navarro JL, Giron J and Vioque E, Amino acid analysis of high-performance liquid chromatography after derivatization with diethyl ethoxymethylenemalonate. J Chromatogr 591: 181-186 (1992).
22. Yust MM, Pedroche J, Girón-Calle J, Alaiz M, Millán F and Vioque J, Production of ACE inhibitory peptides by digestion of chickpea legumin with Alcalase. Food Chem 81: 363-369 (2003).
23. Boye JI, Aksay S, Roufik S, Ribéreau S, Mondor M, Farnworth E, et al, Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques. Food Res Int 43: 537-546 (2010).
24. Salgado PR, Molina Ortiz SE, Petruccelli S and Mauri AN, Sunflower protein concentrates and isolates prepared from oil cakes have high water solubility and antioxidant capacity. J Am Oil Chem Soc 88: 351-360 (2011).
25. Shah J, Lipids, lipases, and lipid-modifying enzymes in plant disease resistance. Annu Rev Phytopathol 43: 229-260 (2005).
26. Blein JP, Coutos-Thévenot P, Marion D and Ponchet M, From elicitins to lipid-transfer proteins: a new insight in cell signalling involved in plant defence mechanisms. Trends Plant Sci 7: 293-296 (2002).
27. Weber H, Fatty acid-derived signals in plants. Trends Plant Sci 7: 217-224 (2002).
28. Morales-de León JC, Vázquez-Mata N, Torres N, Gil-Zenteno L and Bressani R, Preparation and characterization of protein isolate from fresh and hardened beans (Phaseolus vulgaris L.). J Food Sci 72: C96-C102 (2007).
29. Carrasco-Castilla J, Hernández-Álvarez AJ, Jiménez-Martínez C, Jacinto-Hernández C, Alaiz M, Girón-Calle J, et al, Antioxidant and metal chelating activities of Phaseolus vulgaris L. var. Jamapa protein isolates, phaseolin and lectin hydrolysates. Food Chem 131: 1157-1164 (2012).
30. Regente M and De La Canal L, Are storage 2S albumins also defensive proteins? Physiol Mol Plant Pathol 59: 275-276 (2001).
31. Montoya CA, Lallès JP, Beebe S, Montagne L, Souffrant WB and Leterme P, Influence of the Phaseolus vulgaris phaseolin level of incorporation, type and thermal treatment on gut characteristics in rats. Br J Nutr 95: 116-123 (2006).
32. De La Fuente M, Borrajo A, Bermúdez J, Lores M, Alonso J, López M, et al, 2-DE-based proteomic analysis of common bean (Phaseolus vulgaris L.) seeds. J Proteom 74: 262-267 (2011).
33. Li GH, Le GW, Liu H and Shi YH, Mung-bean protein hydrolysates obtained with Alcalase exhibit angiotensin I-converting enzyme inhibitory activity. Food Sci Technol Int 11: 281-287 (2005).
34. Markland FS and Smith EL, Subtilisins: primary structure, chemical and physical properties, in The Enzymes (3rd edn), Vol. 3, ed. by Boyer PD. Academic Press, New York, NY, pp. 561-608 (1971).
35. Pripp AH, Isaksson T, Stepaniak L and Sørhaug T, Quantitative structure-activity relationship modelling of ACE-inhibitory peptides derived from milk proteins. Eur Food Res Technol 219: 579-583 (2004).
36. Ruiz JÁG, Ramos M and Recio I, Angiotensin converting enzyme-inhibitory activity of peptides isolated from Manchego cheese. Stability under simulated gastrointestinal digestion. Int Dairy J 14: 1075-1080 (2004).
37. Joint FAO/WHO/UNU Expert Consultation, Energy and Protein Requirements (WHO Technical Report Series No. 724). World Health Organization, Geneva (1985).