Angiotensin I-Converting Enzyme inhibitory and antioxidant activities and surfactant properties of protein hydrolysates as obtained of Amaranthus hypochondriacus L. grain.

J Soriano-Santos, H Escalona-Buendía
Author Information
  1. J Soriano-Santos: Departamento Biotecnología, Universidad Autónoma Metropolitana-Iztapalapa, Av. San Rafael Atlixco, No. 186, Col. Vicentina, Ap. P. 55-535, Deleg. Iztapalapa, 09340 Mexico City, Mexico.
  2. H Escalona-Buendía: Departamento Biotecnología, Universidad Autónoma Metropolitana-Iztapalapa, Av. San Rafael Atlixco, No. 186, Col. Vicentina, Ap. P. 55-535, Deleg. Iztapalapa, 09340 Mexico City, Mexico.

Abstract

Even though some research has been carried out on surfactant properties of amaranth protein hydrolysates, their bio-functionality has not been studied yet. In this work amaranth grain Alb 1 and Glob were hydrolyzed (Alb 1H, Glob H) and foams and emulsions at optimal conditions (t, E/S, pH5) were prepared in order to assess techno-functional properties such as foaming (F) and emulsifying (E) (capacity (C) and stability (S)). FC and EC were much better for Glob H than for Alb H. Angiotensin I-converting enzyme-inhibitory activity was higher for Alb 1H (roughly 50 %) than that of Glob H (roughly 30 %). Scavenging of radicals activity (DPPH· or ABTS· (+) ) of Alb 1H and Glob H, at 2 mg/mL, was similar (approx. 40 %), but lower than Alb 1 (approx. 70 %), which was the best antioxidant. The low reducing power showed that hydrolysates barely donate an electron or hydrogen. Chelating activity on Cu(2+) was lower than that exhibited by Fe(2+,) which was remarkable, approx. 80 % as long as DH% > 10 %, where hydrolysates displayed high solubility (Alb 1H = 85 %, Glob H = 70 %) because of occurrence of 1-10 kDa peptides. Amaranth foams and emulsions prepared with protein hydrolysates have a potential as a nutraceutical food.

Keywords

References

  1. J Food Sci. 2009 Jun;74(5):H121-6 [PMID: 19646044]
  2. Food Chem. 2008 Nov 15;111(2):370-6 [PMID: 26047437]
  3. Free Radic Biol Med. 1999 May;26(9-10):1231-7 [PMID: 10381194]
  4. J Biotechnol. 2010 Aug 2;148(4):240-7 [PMID: 20561545]
  5. Food Chem. 2012 Dec 1;135(3):1245-52 [PMID: 22953850]
  6. Crit Rev Food Sci Nutr. 2013;53(2):109-25 [PMID: 23072528]
  7. Peptides. 2010 Oct;31(10):1949-56 [PMID: 20600423]
  8. Plant Foods Hum Nutr. 2004 Fall;59(4):169-74 [PMID: 15678726]
  9. Food Chem. 2013 Jan 15;136(2):758-64 [PMID: 23122124]
  10. J Agric Food Chem. 2005 May 4;53(9):3369-76 [PMID: 15853374]
  11. Colloids Surf B Biointerfaces. 2001 Jul;21(1-3):119-124 [PMID: 11377941]
  12. Food Chem. 2012 Dec 1;135(3):1789-95 [PMID: 22953924]
  13. Biochim Biophys Acta. 1994 Jan 11;1204(1):68-74 [PMID: 8305477]
  14. Crit Rev Food Sci Nutr. 2008 May;48(5):430-41 [PMID: 18464032]
  15. Nitric Oxide. 2010 Sep 15;23(2):106-11 [PMID: 20435155]
  16. Phytochemistry. 2009 May;70(7):864-70 [PMID: 19443002]
  17. J Agric Food Chem. 2007 Oct 17;55(21):8703-10 [PMID: 17896813]
  18. Pharm Biol. 2012 Oct;50(10 ):1254-60 [PMID: 22900639]

Word Cloud

Created with Highcharts 10.0.0AlbGlobhydrolysatesHpropertiesprotein1Hactivityapproxsurfactantamaranthgrain1foamsemulsionspreparedAngiotensinroughlylowerantioxidant2+AmaranthEventhoughresearchcarriedbio-functionalitystudiedyetworkhydrolyzedoptimalconditionstE/SpH5orderassesstechno-functionalfoamingFemulsifyingEcapacityCstabilitySFCECmuchbetterI-convertingenzyme-inhibitoryhigher50 %30 %ScavengingradicalsDPPH·ABTS·+2 mg/mLsimilar40 %70 %bestlowreducingpowershowedbarelydonateelectronhydrogenChelatingCuexhibitedFeremarkable80 %longDH% > 10 %displayedhighsolubility1H = 85 %H = 70 %occurrence1-10 kDapeptidespotentialnutraceuticalfoodI-ConvertingEnzymeinhibitoryactivitiesobtainedAmaranthushypochondriacusLACE-inhibitionAntioxidantHydrolysateSurfactant

Similar Articles

Cited By