Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins

Spontón Pablo; Landoni Malena; Couto Alicia; Tonarelli Georgina; Simonetta Arturo

doi:doi:10.11648/j.ijmb.20180303.11

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Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins

Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo

Published in International Journal of Microbiology and Biotechnology (Volume 3, Issue 3)

Received: 27 June 2018 Accepted: 6 August 2018 Published: 12 October 2018

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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.

Published in	International Journal of Microbiology and Biotechnology (Volume 3, Issue 3)
DOI	10.11648/j.ijmb.20180303.11
Page(s)	62-70
Creative Commons	This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited.
Copyright	Copyright © The Author(s), 2018. Published by Science Publishing Group

Keywords

Mannoproteins, Peptides, Glycopeptides, Acetylcholinesterase, Functional Foods

References

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APA Style

Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo. (2018). Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. International Journal of Microbiology and Biotechnology, 3(3), 62-70. https://doi.org/10.11648/j.ijmb.20180303.11

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ACS Style

Spontón Pablo; Landoni Malena; Couto Alicia; Tonarelli Georgina; Simonetta Arturo. Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. Int. J. Microbiol. Biotechnol. 2018, 3(3), 62-70. doi: 10.11648/j.ijmb.20180303.11

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AMA Style

Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo. Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. Int J Microbiol Biotechnol. 2018;3(3):62-70. doi: 10.11648/j.ijmb.20180303.11

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@article{10.11648/j.ijmb.20180303.11,
  author = {Spontón Pablo and Landoni Malena and Couto Alicia and Tonarelli Georgina and Simonetta Arturo},
  title = {Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins},
  journal = {International Journal of Microbiology and Biotechnology},
  volume = {3},
  number = {3},
  pages = {62-70},
  doi = {10.11648/j.ijmb.20180303.11},
  url = {https://doi.org/10.11648/j.ijmb.20180303.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijmb.20180303.11},
  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.},
 year = {2018}
}

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TY  - JOUR
T1  - Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins
AU  - Spontón Pablo
AU  - Landoni Malena
AU  - Couto Alicia
AU  - Tonarelli Georgina
AU  - Simonetta Arturo
Y1  - 2018/10/12
PY  - 2018
N1  - https://doi.org/10.11648/j.ijmb.20180303.11
DO  - 10.11648/j.ijmb.20180303.11
T2  - International Journal of Microbiology and Biotechnology
JF  - International Journal of Microbiology and Biotechnology
JO  - International Journal of Microbiology and Biotechnology
SP  - 62
EP  - 70
PB  - Science Publishing Group
SN  - 2578-9686
UR  - https://doi.org/10.11648/j.ijmb.20180303.11
AB  - 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.
VL  - 3
IS  - 3
ER  -

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Author Information

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
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

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Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo. (2018). Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. International Journal of Microbiology and Biotechnology, 3(3), 62-70. https://doi.org/10.11648/j.ijmb.20180303.11

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ACS Style

Spontón Pablo; Landoni Malena; Couto Alicia; Tonarelli Georgina; Simonetta Arturo. Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. Int. J. Microbiol. Biotechnol. 2018, 3(3), 62-70. doi: 10.11648/j.ijmb.20180303.11

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AMA Style

Spontón Pablo, Landoni Malena, Couto Alicia, Tonarelli Georgina, Simonetta Arturo. Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins. Int J Microbiol Biotechnol. 2018;3(3):62-70. doi: 10.11648/j.ijmb.20180303.11

Copy | Download

@article{10.11648/j.ijmb.20180303.11,
  author = {Spontón Pablo and Landoni Malena and Couto Alicia and Tonarelli Georgina and Simonetta Arturo},
  title = {Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins},
  journal = {International Journal of Microbiology and Biotechnology},
  volume = {3},
  number = {3},
  pages = {62-70},
  doi = {10.11648/j.ijmb.20180303.11},
  url = {https://doi.org/10.11648/j.ijmb.20180303.11},
  eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.ijmb.20180303.11},
  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.},
 year = {2018}
}

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TY  - JOUR
T1  - Peptides and Glycopeptides with Anti-Acetylcholinesterase Activity Obtained from Yeast Mannoproteins
AU  - Spontón Pablo
AU  - Landoni Malena
AU  - Couto Alicia
AU  - Tonarelli Georgina
AU  - Simonetta Arturo
Y1  - 2018/10/12
PY  - 2018
N1  - https://doi.org/10.11648/j.ijmb.20180303.11
DO  - 10.11648/j.ijmb.20180303.11
T2  - International Journal of Microbiology and Biotechnology
JF  - International Journal of Microbiology and Biotechnology
JO  - International Journal of Microbiology and Biotechnology
SP  - 62
EP  - 70
PB  - Science Publishing Group
SN  - 2578-9686
UR  - https://doi.org/10.11648/j.ijmb.20180303.11
AB  - 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.
VL  - 3
IS  - 3
ER  -

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