Effect of purification of galactooligosaccharides derived from lactulose with Saccharomyces cerevisiae on their capacity to bind immune cell receptor Dectin-2. (January 2019)
- Record Type:
- Journal Article
- Title:
- Effect of purification of galactooligosaccharides derived from lactulose with Saccharomyces cerevisiae on their capacity to bind immune cell receptor Dectin-2. (January 2019)
- Main Title:
- Effect of purification of galactooligosaccharides derived from lactulose with Saccharomyces cerevisiae on their capacity to bind immune cell receptor Dectin-2
- Authors:
- Young, Ian D.
Montilla, Antonia
Olano, Agustín
Wittmann, Alexandra
Kawasaki, Norihito
Villamiel, Mar - Abstract:
- Abstract: Lactulose-derived oligosaccharides (OsLu) are prebiotic galactooligosaccharides (GOS) beneficial for human health including immunomodulatory properties; however, the molecular mechanism is unclear. OsLu produced by enzymatic synthesis can be purified with Saccharomyces cerevisiae (OsLu- Sc ). We show that this purification introduces yeast-derived proteins reactive to Dectin-2, an innate immune receptor for fungal polysaccharides. Using a cell-based bioassay, we tested the binding of OsLu and GOS samples to Dectin-2. While OsLu purified with active charcoal and commercial GOS failed to bind to Dectin-2, we found OsLu- Sc bound to this receptor. The carbohydrate-binding incompetent mutant of Dectin-2 failed to bind to OsLu- Sc . These data suggest that OsLu- Sc introduced carbohydrate ligands for Dectin-2. In accordance with this, proteomic analysis revealed OsLu- Sc contained S. cerevisiae -derived mannoproteins. Therefore, our data highlight the importance of the purification method for OsLu, which may positively affect the bioactivity of OsLu. Data are available via ProteomeXchange with identifier PXD010495. Graphical abstract: Unlabelled Image Highlights: Oligosaccharides derived from lactulose (OsLu) were efficiently purified with yeast OsLu treated with Saccharomyces cerevisiae introduced proteins reactive to Dectin-2 Proteomic analysis showed mannoproteins as main responsible for binding to Dectin-2
- Is Part Of:
- Food research international. Volume 115(2019)
- Journal:
- Food research international
- Issue:
- Volume 115(2019)
- Issue Display:
- Volume 115, Issue 2019 (2019)
- Year:
- 2019
- Volume:
- 115
- Issue:
- 2019
- Issue Sort Value:
- 2019-0115-2019-0000
- Page Start:
- 10
- Page End:
- 15
- Publication Date:
- 2019-01
- Subjects:
- Prebiotics -- Oligosaccharides -- Lactulose -- Mannoproteins -- Dectin-2 -- Saccharomyces
CWPs cell wall proteins -- Dectin-2WT wild-type Dectin-2 -- Dectin-2QPD carbohydrate-binding incompetent Dectin-2 mutant -- DM dry matter -- GOS galactooligosaccharides -- OsLu lactose derived oligosaccharides -- OsLu-Sc OsLu purified using Saccharomyces cerevisiae -- OsLu-Sc-S supernatant of OsLu-Sc treated with ethanol -- OsLu-Sc-Pp precipitate of OsLu-Sc treated with ethanol -- OsLu-Sc-R retentate of OsLu-Sc ultrafiltrated -- OsLu-Sc-P permeate of OsLu-Sc ultrafiltrated -- OsLu-ActC OsLu purified with active charcoal -- PSMs peptide spectrum matches
Food -- Analysis -- Periodicals
Food industry and trade -- Periodicals
Food industry and trade -- Canada -- Periodicals
Food Technology -- Periodicals
Food -- Periodicals
Food-Processing Industry -- Periodicals
Aliments -- Industrie et commerce -- Périodiques
Aliments -- Industrie et commerce -- Canada -- Périodiques
Aliments -- Recherche -- Périodiques
Food industry and trade
Canada
Periodicals
Electronic journals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09639969 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodres.2018.07.039 ↗
- Languages:
- English
- ISSNs:
- 0963-9969
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3982.120000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 21494.xml