Antibacterial capacity of lima bean (Phaseolus lunatus L.) peptide fractions obtained by enzymatic hydrolysis.
DOI:
https://doi.org/10.19230/jonnpr.1150Keywords:
Lima bean, Phaseolus lunatus, enzymatic hydrolysis, antibacterial capacity.Abstract
Aim. The aim was to evaluate the antibacterial capacity from lima bean peptide fractions obtained by enzymatic hydrolysis.
Methods. Phaseolus lunatus beans were processed for obtain protein concentrates, which were subjected to enzymatic hydrolysis with pepsin, Flavourzyme and pepsin-pancreatin sequential system. The antibacterial ability against Escherichia coli, Salmonella
typhimurium and Staphylococcus aureus was evaluated for protein hydrolysates with a value less than 10% of degree of hydrolysis
Results. The lower degrees of hydrolysis obtained were: 8.48, 9.58 and 7.40%, for pepsin, Flavourzyme and pepsin-pancreatin sequential system enzyme, respectively. Peptide fractions showed no observable antibacterial ability as growth inhibition of the strains.
Conclusion. Phaseolus lunatus protein hydrolysates showed no antibacterial capacity against the strains studied.
Downloads
References
Rodriguez D, Schöbitz R. Film antimicrobial bases whey protein, lactic acid bacteria incorporated as controller Listeria monocytogenes applied to smoked salmon. Fac. Cienc. Agrop. 2009; 7 (2):49-54.
Davison PM, Harrison MA. Resistence and adaptation to food antimicrobials, sanitizers and other. Food Technol. 2002; 56 (11):69-78.
Gutiérrez P, Orduz S. Péptidos antimicrobianos: estructura, función y aplicaciones. Act. Biol. 2003; 25 (78):5-15.
Mine Y, Shahidi F. Nutraceutical proteins and peptides in health and disease: An overview. En Nutraceutical Proteins and Peptides in Health and Disease; Mine, Y., Shahidi, F., Eds; Taylor & Francis group, 2006; pp. 4-25
Rydlo T, Miltz J, Mor A. Eukaryotic antimicrobial peptides: Promises and premises in food safety. J. Food Sci. 2006; 71 (9):125-135.
Imran M, Revol-Junelles A, René N, Jamshidian M, Akhtar MJ, Arab-Tehrany E, Jacquot M, Stéphane-Desobry S. Microstructure and physico-chemical evaluation of nano-emulsion-based antimicrobial peptides embedded in bioactive packaging films. Food Hydrocoll. 2012;29: 407-419.
Polanco E, Dávila-Ortiz G, Betancur-Ancona D, Chel-Guerrero L. Effects of sequential enzymatic hydrolisis on structural, bioactive and functional properties of Phaseolus lunatus protein isolate. Food Sci.Technol. 2014; 34 (3):441-448.
Córdova-Lizama A, Ruiz-Ruiz J, Segura-Campos M, Betancur-Ancona D, Chel-Guerrero L. Actividad antitrombótica y anticariogénica de hidrolizados proteínicos de frijol lima (Phaseolus lunatus). En pioactividad de péptidos derivados de proteínas alimentarias, Segura Campos, M., Betancur Ancona, D. Chel Guerrero, L. Eds.; Omnia Science, 2013; pp. 123-137.
Chel-Guerrero L, Pérez-Flores V, Betancur-Ancona D, Dávila-Ortiz G. Functional Properties of flours and protein isolates from Phaseolus lunatus and Canavalia ensiformis seeds, J. of Agric. Food Chem. 2002; 50: 584-591.
Association of Official Analytical Chemists (AOAC). (1997). Methods of analysis of association of official analytical chemists. 16 th Edition Washington, D.C.
Domínguez-Magaña M, Segura-Campos M, Dávila-Ortiz G, Betancur-Ancona D, Chel-Guerrero L. ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins, Food Sci. Technol. 2015; 35 (1):167-174.
Pedroche J, Yust MM, Girón-Calle J, Alaiz M, Millán F, Vioque, J. Utilisation of Chickpea protein isolates for production of peptides with angiotensin- I converting enzyme (ACE)-inhibitory activity. J. Sci. Food Agric. 2002;82: 960-965.
Nielsen P, Petersen D, Dambmann C. Improved method for determining food protein degree of hydrolysis. J. Food Sci. Food Chem. Toxicol. 2001; 66 (5):642-646.
Lowry OH, Rosebrough NJ, Farr L, Randall RJ. Protein measurement with the folin phenol reagent. J. of Biol. Chem. 1951; 193:267-275
Chim-Chi Chim YA, Martínez AA, Chel-Guerrero L. Caracterización de hidrolizados de Jatropha curcas y Vigna unguiculata. EAE Editorial Academia Espanola, USA 2013
Corona A, Jiménez R. Comparación de dos métodos de siembra para el recuento de microorganismos en muestras con alta concentración microbiana. Rev. Fac. Ing. Quím. 2004; 40:3-7.
Montgomery, D. C. Diseño y análisis de experimentos. 2da Ed. Editorial Limusa. México, D. F. 2006.
Betancur-Ancona D, Martínez-Rosado R, Corona-Cruz A, Castellanos-Ruelas A, Jaramillo-Flores M, Chel-Guerrero L. Functional properties of hydrolysates from Phaseolus lunatus seeds. Int. J. Food Sci. Technol. 2009;44 (1): 128-137.
Benitez R, Ibarz A, Pagan J. Hidrolizados de proteína: Procesos y aplicaciones. Acta Bioq. Clin. Lat. 2008; 42(2):227-236.
Marrufo-Estrada DM, Segura-Campos MR, Chel-Guerrero LA., Betancur-Ancona DA. Defatted Jatropha curcas flour and protein isolate as materials for protein hydrolysates with biological activity. Food Chem. 2013; 138:77-83.
Corzo-Ríos L, Chel-Guerrero L, Betancur-Ancona D. Extracción de las fracciones de almidón y proteína del grano de la leguminosa Mucuna pruriens. Technol. Cienc. Educ. 2000; 15 (1):37-41.
Betancur-Ancona D, Gallegos-Tintore S, Chel-Guerrero, L. Wet-fractionation of Phaseolus lunatus seeds: partial characterization of starch and protein. J. Sci. Food Agric. 2004; 84: 1193-1201.
Tsumura K, Saito T, Tsuge K, Ashida H, Kugimiya W, Inouye K. Functional properties of soy hydrolysates obtained by selective proteolysis. LWT-Food Sci Tech. 2005: 38: 255-261.
Paraman I, Hettiarachchy NS, Schaefer C, Beck MI. Hydrophobicity, solubility and emulsifying properties of enzime-modified rice endosperm protein. Cereal Chem. 2007; 84(4): 343-349.
Megías C, Pedroche J, Yust MM, Alaiz M, Girón-Calle, J. Millán F, Vioque J. Sunflower protein hydrolysates reduce cholesterol micellar solubility. Plants Foods Hum. Nutr. 2009; 64: 86-93.
Picot L, Ravallec R, Fouchereu-Péron M, Vandanjon L, Jaouen P, Chaplain-Derouiniot M, Guérard F, Chabeaud A, LeGal Y, Martinez O, Bergé JP, Piot J, M., Batista I, Pires C, Thorkelsson G, Delannoy C,
Jakobsen G, Johansson I, Bourseau P. Impact of ultrafiltration and nanoiltration of an industrial fish protein hydrolysate on its bioactive properties. J. Sci. Food and Agric. 2010; 90 (11): 1819-1826
Sornwatana T, Roytrakul S, Wetprasit N, Ratanapo S. A new antimicrobial peptide from digestion of Brucea amarissima Desv fruit protein. 36th Congress on Science and Technology of Thailand. 2010; pp. 1-4.
Bojórquez-Balam E, Ruiz-Ruiz J, Segura-Campos M, Betancur-Ancona D, Chel-Guerrero L. Evaluación de la capacidad antimicrobiana de fracciones peptídicas de hidrolizados proteínicos de frijol lima (Phaseolus lunatus). M. Segura- Campos, L. Chel Guerrero, D. Betancur Ancona (Eds.), Bioactividad de péptidos derivados de proteínas alimentarias. Barcelona: OmniaScience. 2013; pp. 139-154.
Additional Files
Published
Issue
Section
License
All accepted originals remain the property of JONNPR. In the event of publication, the authors exclusively transfer their rights of reproduction, distribution, translation and public communication (by any sound, audiovisual or electronic medium or format) of their work. To do so, the authors shall sign a letter transferring these rights when sending the paper via the online manuscript management system.
The articles published in the journal are freely used under the terms of the Creative Commons BY NC SA license, therefore.
You are free to:
Share — copy and redistribute the material in any medium or format
Adapt — remix, transform, and build upon the material
The licensor cannot revoke these freedoms as long as you follow the license terms.
Under the following terms:
Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
NonCommercial — You may not use the material for commercial purposes.
ShareAlike — If you remix, transform, or build upon the material, you must distribute your contributions under the same license as the original.
No additional restrictions — You may not apply legal terms or technological measures that legally restrict others from doing anything the license permits.

This work is licensed under a Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International License


















