4.7 Article

Pea Protein Extraction Assisted by Lactic Fermentation: Impact on Protein Profile and Thermal Properties

期刊

FOODS
卷 10, 期 3, 页码 -

出版社

MDPI
DOI: 10.3390/foods10030549

关键词

pea protein; alkaline solubilization; isoelectric precipitation; extraction; lactic acid fermentation; thermal properties

资金

  1. French Agence Nationale de la Recherche (ANR PEAVALUE project) [ANR-19-CE21-0008-03]
  2. European Regional Development Fund (FEDER-FSE Bourgogne 2014/2020) [BG0025913]
  3. Agence Nationale de la Recherche (ANR) [ANR-19-CE21-0008] Funding Source: Agence Nationale de la Recherche (ANR)

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The study aimed to explore an alternative extraction method based on alkaline extraction/isoelectric precipitation for improving the solubility of pea protein, finding that fermentation-assisted extraction can increase protein yield and content. The results indicated that lactic acid bacteria enhanced protein extraction and quality through fermentation activity.
Although pea protein has been widely explored, its consumption is still limited by undesirable sensory characteristics and low solubility. All these properties can be modified during protein extraction process. Besides, previous studies showed that lactic acid bacteria (LAB) have a positive effect on legume protein ingredients in terms of flavor and functional properties. Hence, the objective of this work was to explore an alternative extraction method based on alkaline extraction/isoelectric precipitation (AEIEP) resulting in globulin-rich and residual albumin-rich fractions. Here, the decrease in pH was achieved by lactic fermentation instead of mineral acid addition. Different bacteria strains (Streptococcus thermophilus, Lactobacillus acidophilus and Bifidobacterium lactis) have been used alone or in co-culture, and the results were compared with the usual acidification. The extraction assisted by fermentation led to the increase by 20-30% in protein content/yield of the albumin fraction, meaning that the solubility of the extracted pea protein was increased. This result could be explained by the proteolytic activity of bacteria during lactic fermentation. Therefore, the thermal denaturation properties of the isolated protein fractions measured by differential scanning calorimetry could be mainly ascribed to differences in their polypeptide compositions. In particular, higher denaturation enthalpy in globulin fractions after fermentation compared to AEIEP (similar to 15 J/g protein vs. similar to 13 J/g protein) revealed the relative enrichment of this fraction in pea legumins; a higher part of 7S globulins seemed to be consumed by lactic acid bacteria.

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