Table 3 Stability and/or bioaccessibility of bioactive peptides and/or bioactive properties after simulated in vitro gastrointestinal tract (GIT) digestion of fermented legumes
Legumes or their extracts or products | Microorganism/ enzymes | Fermentation conditions (pH, temperature, time) | GIT enzymes used | Bioactive properties after GIT digestion | Important associated peptides and their parent protein and peptide molecular mass | References |
|---|---|---|---|---|---|---|
Lentils seeds | Lactobacillus plantarum with Savinase | 8.5; 37 °C; 15 h | Pepsin, pancreatin | Angiotensin -I- converting enzyme (ACE) inhibitory activity (IC50 0.23 mg/mL), α-sucrase inhibitory activity (39%) was present but reduced, antioxidant activity (oxygen radical absorbance capacity (ORAC)); increased radical oxygen species (ROS) production inhibition; maltase activity and lipase inhibition were lost | SGREKWERKEDEEKVVEEEEGEWRGS, KDVVPEWVRIGFS, LNTKYDTIEKVLLEEQENEPH, LVNPDDEEDLRVVDF, SLNTKYDTIEKVLLEQENEPH, FNTDYEEIEKVLL, FNTEYEEIEKVLLEEQEQKSQ, KDVVPEWVRIGFSA and more. Peptide sequence derived from convicilin, vicilin (allergen Len c 1.0101 and 1.0102) and lectin 1.1–3.2 kDa | (Bautista-Expósito et al., 2018) |
Lentils (Pardina and Castellana) seeds and flour (Lens culinaris) | Pleurotus ostreatus | pH not reported; 28 °C; 14 days | Amylase, pepsin, pancreatin-bile salts | ACE inhibitory activity (%) was present and substantially increased (from approx. 8–15% up to 70%) but was similar or lower than unfermented products, indicating that the net inhibitory activity derived during fermentation was lost | Associated peptides not identified 0.45 kDa, 1.4 kDa and ≥ 12.5 kDa | (Sánchez-GarcÃa et al., 2024) |
Bean seeds (Phaseolus vulgaris L.) (dehulled) | Lactobacillus plantarum 299v | pH not reported; 22 °C, 30 °C and 37 °C; 3 h, 3 days and 7 days | α-Amylase, pepsin, pancreatin | ACE inhibitory activity (IC50 0.28–7.65 mg/mL), and anti-lipase inhibitory activity (1.19–6.25 mg/mL) were present depending on fermentation conditions | INEGSLLLPH, FVVAEQAGNEEGFE, SGGGGGGVAGAATASR, GSGGGGGGGFGGPRR, GGYQGGGYGGNSGGGYGNRG, GGSGGGGGSSSGRRP, GDTVTVEFDTFLSR. Peptide sequence derived from vicilin, legumin J-like 3.5–7.0 kDa | (Jakubczyk et al., 2017) |
Lima beans (Phaseolus lunatus L.) | Rhizopus oligosporus | pH not reported; room temperature; 36 h soaking before 48 h fermentation | Pepsin, pancreatin | ACE inhibitory activity was present and was slightly increased (up to IC50 0.59 mg/mL) | Associated peptides not identified  < 1 kDa (majorly), 1–3 kDa, 3.5–14 kDa | (Pertiwi et al., 2020) |
Faba bean seeds (Vicia faba L. var.) | Lactobacillus plantarum 299v | pH not reported; 22 °C, 30 °C and 37 °C; 12 h soaking before 3 h, 3 days and 7 days fermentation | α-Amylase, pepsin, pancreatin | Antiradical activity against ABTS (IC50 3.51–0.99 mg/mL), ACE (IC50 2.9–1.01 mg/mL), Lipoxidase (IC50 2.90–0.54 mg/mL) and lipase (IC50 2.31–0.89 mg/mL) inhibitory activities were present depending on the fermentation conditions | DALEPDNRIESEGGLIETWNPNNRQ, FEEPQQSEQGEGR, GSRQEEDEDEDE, WMYNDQDIPVINNQLDQMPR, RGEDEDDKEKRHSQKGES, RLNIGSSSSPDIYNPQAGR. Peptide sequence derived from N-terminal legumin A1 prepro-polypeptide | (Jakubczyk et al., 2019) |
Common bean (Phaseolus vulga L.) milk and yogurt | Bifidobacterium bifidum, Lactobacillus spp, Streptococcus thermophilus | Up to 4.5; room temperature, 4–14 h | Pepsin, pancreatin | Cellular antioxidant activity (peroxyl radicals quenching ability) (IC50 0.1–0.5 mg/mL), and cellular anti-inflammatory activity, i.e., inhibition of IL-8 secretion induced by TNF-α were present | γ-glutamyl-S-methylcysteine, γ-glutamyl-leucine, Xle-Val-Xle  < 10 kDa and 10–50 kDa | (Chen et al., 2019) |
Black bean tempeh | R. oligosporus | pH not reported; 35 °C; 39 h | Amylase, pepsin, trypsin | ACE inhibitory activity (%) was present and substantially increased (from approx. 30% up to 83%) but was lower than unfermented products indicating that some ACE inhibitory activity was lost due to fermentation | Associated peptides not identified  < 10 kDa and ≤ 22 kDa | (Wang et al. ,2022) |
Pea seeds (Pisum sativum var. Bajka) protein | Lactobacillus plantarum 299v | pH not reported; 22 °C, 30 °C and 37 °C; 12 h soaking before 3 h, 3 days and 7 days fermentation | α-Amylase, pepsin, pancreatin | ACE inhibitory activity was present (IC50 0.48–0.19 mg/mL). Further isolation of peptide fractions yielded lower IC50 values of 0.064–0.14 mg/mL | KEDDEEEEQGEEE, parent protein not reported. < 1.6 kDa and < 7 kDa | (Jakubczyk et al., 2013) |
Pea protein isolates | Lactobacillus helveticus and/or Saccharomyces cerevisiae | 6.1–3.5; 37 °C; 48 h | Pepsin, trypsin, α-chymotrypsin | ACE inhibitory activity was present (IC50 0.11–0.23 mg/mL) but similar to unfermented peas, suggesting that the net ACE inhibitory activity derived during fermentation was lost | Associated peptides not identified 3 kDa | (Vermeirssen et al., 2003) |