Bacteria do it better! Proteomics suggests the molecular basis for improved digestibility of sourdough products. (15th October 2021)
- Record Type:
- Journal Article
- Title:
- Bacteria do it better! Proteomics suggests the molecular basis for improved digestibility of sourdough products. (15th October 2021)
- Main Title:
- Bacteria do it better! Proteomics suggests the molecular basis for improved digestibility of sourdough products
- Authors:
- Reale, Anna
Di Stasio, Luigia
Di Renzo, Tiziana
De Caro, Salvatore
Ferranti, Pasquale
Picariello, Gianluca
Addeo, Francesco
Mamone, Gianfranco - Abstract:
- Graphical abstract: Highlights: The peptide profiles of sourdough vary among different fermenting lactobacilli. β-amylase, triticin and serpin are primary proteolytic targets in sourdough. Proteolysis in sourdough moderately affects the gluten structure. Celiac disease immunotoxic peptides are resistant to proteolysis. Proteolysis of β-amylase could in part explain the decrease of fermentable sugars. Abstract: The aim of this study was to evaluate the dynamics of proteolysis during dough fermentation started with different lactic acid bacteria species, through the identification of intermediate and small-sized peptides generated during fermentation. Single-strain cultures of Levilactobacillus brevis, Fructilactobacillus sanfranciscensis, Companilactobacillus alimentarius, and Leuconostoc pseudomesenteroides were assayed as sourdough starters. Assays were carried out at lab-scale for 48 h of fermentation, using both unstarted and yeast-leavened dough as controls. Physicochemical and microbiological analyses were combined with peptidomic and proteomic profiling, identifying several hundreds of peptides mainly released from the water-soluble wheat proteins, including β-amylase, triticin, and serpins. Both α- and γ-gliadins were hydrolyzed, though only at the N -terminal domain, while the central protein region – encrypting celiac disease epitopes– remained unaffected. The bacterial-mediated consumption of sugars and the concomitant hydrolysis of starch degrading β-amylase couldGraphical abstract: Highlights: The peptide profiles of sourdough vary among different fermenting lactobacilli. β-amylase, triticin and serpin are primary proteolytic targets in sourdough. Proteolysis in sourdough moderately affects the gluten structure. Celiac disease immunotoxic peptides are resistant to proteolysis. Proteolysis of β-amylase could in part explain the decrease of fermentable sugars. Abstract: The aim of this study was to evaluate the dynamics of proteolysis during dough fermentation started with different lactic acid bacteria species, through the identification of intermediate and small-sized peptides generated during fermentation. Single-strain cultures of Levilactobacillus brevis, Fructilactobacillus sanfranciscensis, Companilactobacillus alimentarius, and Leuconostoc pseudomesenteroides were assayed as sourdough starters. Assays were carried out at lab-scale for 48 h of fermentation, using both unstarted and yeast-leavened dough as controls. Physicochemical and microbiological analyses were combined with peptidomic and proteomic profiling, identifying several hundreds of peptides mainly released from the water-soluble wheat proteins, including β-amylase, triticin, and serpins. Both α- and γ-gliadins were hydrolyzed, though only at the N -terminal domain, while the central protein region – encrypting celiac disease epitopes– remained unaffected. The bacterial-mediated consumption of sugars and the concomitant hydrolysis of starch degrading β-amylase could underlie improved digestibility and several nutritionally beneficial effects of sourdough baked products. … (more)
- Is Part Of:
- Food chemistry. Volume 359(2021)
- Journal:
- Food chemistry
- Issue:
- Volume 359(2021)
- Issue Display:
- Volume 359, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 359
- Issue:
- 2021
- Issue Sort Value:
- 2021-0359-2021-0000
- Page Start:
- Page End:
- Publication Date:
- 2021-10-15
- Subjects:
- Sourdough -- Proteolysis -- β-amylase -- Gluten proteins -- Lactic acid bacteria
Food -- Analysis -- Periodicals
Food -- Composition -- Periodicals
664 - Journal URLs:
- http://www.sciencedirect.com/science/journal/03088146 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodchem.2021.129955 ↗
- Languages:
- English
- ISSNs:
- 0308-8146
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 3977.284000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 17223.xml