Degradation of HMW glutenins during wheat sourdough fermentations

Jussi Loponen (Corresponding Author), Markku Mikola, Kati Katina, Tuula Sontag-Strohm, Hannu Salovaara

Research output: Contribution to journalArticleScientificpeer-review

60 Citations (Scopus)

Abstract

Bakeries use sourdoughs to improve bread properties such as flavor and shelf life. The degradation of gluten proteins during fermentation may, however, crucially alter the gluten network formation. We observed changes that occurred in the HMW glutenins during wheat sourdough fermentations. As fermentation starters, we used either rye sourdough or pure cultures of lactobacilli and yeast. In addition, we incubated wheat flour (WF) in the presence of antibiotics under different pH conditions. The proteolytic activities of cereal and sourdough‐derived proteinases were studied with edestin and casein. During sourdough fermentations, most of the highly polymerized HMW glutenins degraded. A new area of alcohol‐soluble proteins (≈30.000 MW) appeared as a result of the proteolytic breakdown of gluten proteins. Very similar changes were observable as WF was incubated in the presence of antibiotics at pH 3.7. Cereal and sourdough‐derived proteinases hydrolyzed edestin at pH 3.5 but showed no activity at pH 5.5. An aspartic proteinase inhibitor (pepstatin A) arrested 88–100% of the activities of sourdough enzymes. According to these results, the most active proteinases in wheat sourdoughs were the cereal aspartic proteinases. Acidic conditions present in sourdoughs create an ideal environment for cereal aspartic proteinases to be active against gluten proteins.
Original languageEnglish
Pages (from-to)87 - 93
Number of pages7
JournalCereal Chemistry
Volume81
Issue number1
DOIs
Publication statusPublished - 2004
MoE publication typeA1 Journal article-refereed

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sourdough
Glutens
glutenins
Aspartic Acid Proteases
Fermentation
Triticum
fermentation
Degradation
wheat
Peptide Hydrolases
degradation
gluten
aspartic proteinases
Flour
Bakeries
Anti-Bacterial Agents
proteinases
Starters
Flavors
Bread

Cite this

Loponen, J., Mikola, M., Katina, K., Sontag-Strohm, T., & Salovaara, H. (2004). Degradation of HMW glutenins during wheat sourdough fermentations. Cereal Chemistry, 81(1), 87 - 93. https://doi.org/10.1094/CCHEM.2004.81.1.87
Loponen, Jussi ; Mikola, Markku ; Katina, Kati ; Sontag-Strohm, Tuula ; Salovaara, Hannu. / Degradation of HMW glutenins during wheat sourdough fermentations. In: Cereal Chemistry. 2004 ; Vol. 81, No. 1. pp. 87 - 93.
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Loponen, J, Mikola, M, Katina, K, Sontag-Strohm, T & Salovaara, H 2004, 'Degradation of HMW glutenins during wheat sourdough fermentations', Cereal Chemistry, vol. 81, no. 1, pp. 87 - 93. https://doi.org/10.1094/CCHEM.2004.81.1.87

Degradation of HMW glutenins during wheat sourdough fermentations. / Loponen, Jussi (Corresponding Author); Mikola, Markku; Katina, Kati; Sontag-Strohm, Tuula; Salovaara, Hannu.

In: Cereal Chemistry, Vol. 81, No. 1, 2004, p. 87 - 93.

Research output: Contribution to journalArticleScientificpeer-review

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AU - Mikola, Markku

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PY - 2004

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N2 - Bakeries use sourdoughs to improve bread properties such as flavor and shelf life. The degradation of gluten proteins during fermentation may, however, crucially alter the gluten network formation. We observed changes that occurred in the HMW glutenins during wheat sourdough fermentations. As fermentation starters, we used either rye sourdough or pure cultures of lactobacilli and yeast. In addition, we incubated wheat flour (WF) in the presence of antibiotics under different pH conditions. The proteolytic activities of cereal and sourdough‐derived proteinases were studied with edestin and casein. During sourdough fermentations, most of the highly polymerized HMW glutenins degraded. A new area of alcohol‐soluble proteins (≈30.000 MW) appeared as a result of the proteolytic breakdown of gluten proteins. Very similar changes were observable as WF was incubated in the presence of antibiotics at pH 3.7. Cereal and sourdough‐derived proteinases hydrolyzed edestin at pH 3.5 but showed no activity at pH 5.5. An aspartic proteinase inhibitor (pepstatin A) arrested 88–100% of the activities of sourdough enzymes. According to these results, the most active proteinases in wheat sourdoughs were the cereal aspartic proteinases. Acidic conditions present in sourdoughs create an ideal environment for cereal aspartic proteinases to be active against gluten proteins.

AB - Bakeries use sourdoughs to improve bread properties such as flavor and shelf life. The degradation of gluten proteins during fermentation may, however, crucially alter the gluten network formation. We observed changes that occurred in the HMW glutenins during wheat sourdough fermentations. As fermentation starters, we used either rye sourdough or pure cultures of lactobacilli and yeast. In addition, we incubated wheat flour (WF) in the presence of antibiotics under different pH conditions. The proteolytic activities of cereal and sourdough‐derived proteinases were studied with edestin and casein. During sourdough fermentations, most of the highly polymerized HMW glutenins degraded. A new area of alcohol‐soluble proteins (≈30.000 MW) appeared as a result of the proteolytic breakdown of gluten proteins. Very similar changes were observable as WF was incubated in the presence of antibiotics at pH 3.7. Cereal and sourdough‐derived proteinases hydrolyzed edestin at pH 3.5 but showed no activity at pH 5.5. An aspartic proteinase inhibitor (pepstatin A) arrested 88–100% of the activities of sourdough enzymes. According to these results, the most active proteinases in wheat sourdoughs were the cereal aspartic proteinases. Acidic conditions present in sourdoughs create an ideal environment for cereal aspartic proteinases to be active against gluten proteins.

U2 - 10.1094/CCHEM.2004.81.1.87

DO - 10.1094/CCHEM.2004.81.1.87

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JF - Cereal Chemistry

SN - 0009-0352

IS - 1

ER -

Loponen J, Mikola M, Katina K, Sontag-Strohm T, Salovaara H. Degradation of HMW glutenins during wheat sourdough fermentations. Cereal Chemistry. 2004;81(1):87 - 93. https://doi.org/10.1094/CCHEM.2004.81.1.87