International Journal of Microbiology and Biotechnology

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

Received: 27 June 2018    Accepted: 06 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.

DOI 10.11648/j.ijmb.20180303.11
Published in International Journal of Microbiology and Biotechnology (Volume 3, Issue 3, September 2018)
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), 2024. Published by Science Publishing Group

Keywords

Mannoproteins, Peptides, Glycopeptides, Acetylcholinesterase, Functional Foods

References
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Author Information
  • 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

  • Center of Investigations in Hydrates of Carbon, National Council of Scientific and Technical Investigations, University of Buenos Aires, Buenos Aires, Argentina

  • Center of Investigations in Hydrates of Carbon, National Council of Scientific and Technical Investigations, University of Buenos Aires, Buenos Aires, Argentina

  • Department of Organic Chemistry, Bioactive Peptide Laboratory, School of Biochemistry and Biological Sciences, National University of the Litoral, Santa Fe, Argentina

  • Department of Food Technology and Biotechnology, Laboratory of Microbiology and Biotechnology, School of Chemical Engineering, National University of the Litoral, Santa Fe, Argentina

Cite This Article
  • 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://download.sciencepg.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
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    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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