Volume 3, Issue 3, September 2018, Page: 62-70
Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins
Spontón Pablo, Department of Food Technology and Biotechnology, Laboratory of Microbiology and Biotechnology, School of Chemical Engineering, National University of the Litoral, Santa Fe, Argentina; Department of Organic Chemistry, Bioactive Peptide Laboratory, School of Biochemistry and Biological Sciences, National University of the Litoral, Santa Fe, Argentina
Landoni Malena, Center of Investigations in Hydrates of Carbon, National Council of Scientific and Technical Investigations, University of Buenos Aires, Buenos Aires, Argentina
Couto Alicia, Center of Investigations in Hydrates of Carbon, National Council of Scientific and Technical Investigations, University of Buenos Aires, Buenos Aires, Argentina
Tonarelli Georgina, Department of Organic Chemistry, Bioactive Peptide Laboratory, School of Biochemistry and Biological Sciences, National University of the Litoral, Santa Fe, Argentina
Simonetta Arturo, Department of Food Technology and Biotechnology, Laboratory of Microbiology and Biotechnology, School of Chemical Engineering, National University of the Litoral, Santa Fe, Argentina
Received: Jun. 27, 2018;       Accepted: Aug. 6, 2018;       Published: Oct. 12, 2018
DOI: 10.11648/j.ijmb.20180303.11      View  183      Downloads  22
Abstract
Purified mannoproteins from 5 yeast strains belonging to the genera Brettanomyces, Candida, Pichia and Saccharomyces were studied. Each mannoprotein extract was hydrolysed with proteolytic enzymes, generating small peptides whose inhibitory activity against acetylcholinesterase (AChE) was determined. Partial purification of six selected mannoprotein extracts was done by reversed phase chromatography, six fractions with relevant inhibitory activity being obtained. Chromatographic and spectroscopic analyses revealed mainly hydrophilic peptides, with molecular weight between 700 and 4800 Da. The presence of sugars in all fractions was determined, mannose being the most abundant one. Subsequently, the most active fractions were again separated by affinity chromatography, which led to two new types of fractions: peptidic fractions (PFs) and glycopeptidic fractions (GPFs). Results showed that all fractions inhibited AChE, although GPFs inhibited AChE to a greater degree than PFs, with a percentage of inhibition ranging from 49.3 to 77.8%. Likewise, all GPFs fractions had higher values of inhibition than the corresponding whole fraction, while PFs showed lower percentages of anti-acetylcholinesterase activity. These results suggest that glycopeptidic are the most interesting fractions for their ability to inhibit this enzyme. As a conclusion, it was shown that some peptides produced by hydrolysis of mannoproteins proved able to inhibit AChE and should be considered as potential anti-AChE agents and significant to the manufacturing of food with potential functional properties.
Keywords
Mannoproteins, Peptides, Glycopeptides, Acetylcholinesterase, Functional Foods
To cite this article
Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo, Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins, International Journal of Microbiology and Biotechnology. Vol. 3, No. 3, 2018, pp. 62-70. doi: 10.11648/j.ijmb.20180303.11
Copyright
Copyright © 2018 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/) which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Reference
[1]
Sung, W. S.; Park, Y.; Choi, C. H.; Hahm, K. S. and Lee D. G. (2007) Mode of antibacterial action of a signal peptide, Pep27 from Streptococcus pneumoniae. Biochemical Biophysical Research Communications, 363 (3): 806-810.
[2]
Duval, E.; Zatylny, C.; Laurencin, M.; Baudy-Floc’h, M. and Henry, J. (2009) KKKKPLFGLFFGLF: a cationic peptide designed to exert antibacterial activity. Peptides, 30 (9): 1608–1612.
[3]
Lin, P. and Ng, T. B. (2008) A novel and exploitable antifungal peptide from kale (Brassica alboglabra) seeds. Peptides, 29 (10): 1664-1671.
[4]
Pan, Y.; Lee, A.; Wan, J.; Coventry, M. J.; Michalski, W. P.; Shiell, P. and Roginski, H. (2006) Antiviral properties of milk proteins and peptides. International Dairy Journal, 16 (11): 1252-1261.
[5]
Rockwood, K.; Bouchard, R. W.; Camicioli, R. and Le´ger, G. (2007) Toward a revision of criteria for the dementias. Alzheimers Dement, 3 (4): 428-440.
[6]
Grinberg, L. T. and Heinsen, H. (2010) Toward a pathological definition of vascular dementia. Journal of Neurological Sciences, 299 (1-2): 136-138.
[7]
Caroli, A. and Frisoni, G. B. (2010) The dynamics of Alzheimer’s disease biomarkers in the Alzheimer’s disease neuroimaging initiative cohort. Neurobiology of Aging, 31 (8): 1263-1274.
[8]
Swerdlow, R. H. (2011) Brain aging, Alzheimer’s disease, and mitochondria. Biochimicaet Biophysica Acta, 1812 (12): 1630-1639.
[9]
Kettl, P. (2007) Helping families with end-of-life care in Alzheimer's disease. Journal Clinical Psychiatry, 68 (3): 428-429.
[10]
Singh, A. P. (2003) The role of natural products in pharmacotherapy of Alzheimer disease. Ethnobotanical Leaflets, 7: 1-5.
[11]
Keane, S. and Ryan, M. F. (1999) Purification, characterization, and inhibition by monoterpenes of acetylcholinesterase from the wax moth, Galleria Mellonella. Insect Biochemistry and Molecular Biology, 29: 1097-1104.
[12]
Filho, J.; Medeiros, K.; Diniz, M.; Batista, L.; Athayde-Filho, P. and Silva, M. (2006) Natural products inhibitors of the enzyme acetylcholinesterase. Revista Brasileira de Pharmacognosia, 16: 258-285.
[13]
Pulok, K. M.; Venkatesan, K.; Mainak, M. and Houghton, P. J. (2007) Acetylcholinesterase inhibitors from plants. Phytomedicine, 14: 289-300.
[14]
Kantor, D. (2007) Enfermedad de Alzheimer. Review provided by VeriMed Healthcare NetYork. Medline plus enciclopediamédica. http://www.nlm.nih.gov/medlineplus/spanish/ency/article/000760.htm
[15]
Murray, A. P.; Faraoni, M. B.; Castro, M. J.; Alza, N. P. and Cavallaro, V. (2013) Natural AChE inhibitors from plants and their contribution to Alzheimer’s disease therapy. Current Neuropharmacology, 11: 388-413.
[16]
Ahn, C. B.; Lee, K. H. and Je, J. Y. (2010) Enzymatic production of bioactive protein hydrolysates from tuna liver: effect of enzymes and molecular weight on bioactivity. International Journal of Food Science and Technology, 45: 562-568.
[17]
Patocka, J. (2012) Natural cholinesterase inhibitors from mushrooms. Military Medical Science Letters, 81 (1): 40-44.
[18]
Custódio, L.; Justo, T.; Silvestre, L.; Barradas, A.; Duarte, C. V.; Pereira, H.; Barreira, L.; Rauter, A. P.; Alberício, F. and Varela, J. (2012) Microalgae of different phyla display antioxidant, metal chelating and acetylcholinesterase inhibitory activities. Food Chemistry, 131: 134-140.
[19]
Núñez, Y. P .; Carrascosa, A. V.; González, R.; Polo, M. C. and Martínez Rodríguez, A. J. (2006) Isolation and characterization of a thermally extracted yeast cell wall fraction potentially useful for improving the foaming properties of sparkling wines. Journal of Agriculture and Food Chemistry, 54: 7898-7903.
[20]
Spontón, P. G.; Spinelli, R.; Drago, S. R.; Tonarelli, G. G. and Simonetta, A. C. (2016) Acetylcholinesterase-inhibitor hydrolysates obtained from ‘in vitro’ enzymatic hydrolysis of mannoproteins extracted from different strains of yeasts. International Journal of Food Science and Technology, 51, 300-308.
[21]
Peat, S.; Whelan, W. J. and Edwards, T. E. (1961). Polysaccharides of baker's yeast. Part IV. Mannan. Journal of Chemical Society, (London): 28-35.
[22]
Cameron, D.; Cooper, D. and Neufeld R. (1988) The mannoprotein of Saccharomyces cerevisiae is an effective bioemulsifier. Applied and Environmental Microbiology, 54: 1420-1425.
[23]
Ellman, G. L.; Courtney, K. D.; Andres, V. Jr. and Feather-Stone, R. M. (1961) A new and rapid colorimetric determination of acetylcholinesterase activity. Biochemical Pharmacology, 7: 88-95.
[24]
López, S., Bastida, J., Viladomat, F. and Codina, C. (2002). Acetylcholinesterase inhibitory activity of some Amaryllidaceae alkaloids and Narcissus extracts. Life Sciences, 71, 2521-2529.
[25]
Hardy, M. R. and Townsend R. R. (1994) High-pH anion-exchange chromatography of glycoprotein-derived carbohydrates. Methods Enzymology, 230: 208-225.
[26]
Gañan, M.; Carrascosa, A. V.; de Pascual-Teresa, S. andMartínez-Rodríguez, A. J. (2009) Inhibition by yeast-derived mannoproteins of adherence to and invasion of Caco-2 cells by Campylobacter jejuni. Journal of Food Protection, 72: 55-59.
[27]
Dikit, P. S. M.; Musikasang, H. and Kittikun A. H. (2010) Emulsifier properties of the mannoprotein extract from yeast isolated from sugar palm wine. ScienceAsia, 36: 312-318.
[28]
Wang, W. and de Mejia, E. G. (2005). A new frontier in soy bioactive peptides that may prevent age-related diseases. Comprehensive Reviews in Food Science and Food Safety, 4: 63-78.
[29]
Zare-Zardini, H.; Tolueinia, B.; Hashemi, A.; Ebrahimi, L. and Fesahat, F. (2013). Antioxidant and cholinesterase inhibitory activity of a new peptide from Ziziphus jujuba fruits. American Journal of Alzheimer's Disease and Other Dementias, 28 (7): 702-709.
[30]
Rafiquzzaman, S. M.; Kim, E. Y.; Lee, J. M.; MdMohibbullah; MdBadrulAlam; Moon, I. S.; Kim, J. M. and Kong, I. S. (2015) Anti-Alzheimers and antiinflammatory activities of a glycoprotein purified from the edible brown alga Undariapinnatifida. Food Research International, 77: 18-124.
[31]
Tsai, C. H.; Yen, Y. H. and Yang, J. P. W. (2015) Finding of polysaccharide-peptide complexes in Cordyceps militaris and evaluation of its acetylcholinesterase inhibition activity. Journal of Food and Drug Analysis, 23: 63-70.
[32]
Karlsson, E.; Mbugua, P. M. and Rodriguez-Itthurralde, D. (1984) Fasciculins, anticholinesterase toxins from the venom of the green mamba Dendroaspis angusticeps. Journal of Physiology, 79: 232-240.
[33]
Kafurke, U.; Erijman, A.; Aizner, Y.; Shifman, J. M. and Eichlera, J. (2015) Synthetic peptides mimicking the binding site of human acetylcholinesterase for its inhibitor fasciculin 2. Journal of Peptide Sciences, 21 (9): 723-730.
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