Peptides and isoflavones in gastrointestinal digests contribute to the anti-inflammatory potential of cooked or germinated desi and kabuli chickpea (Cicer arietinum L.)

Abstract

It is largely unknown how processing affects bioactive potential of chickpea proteins to prevent bowel inflammatory diseases. The aim was to investigate the anti-inflammatory activity of protein concentrates from germinated and cooked chickpeas (GC and CC, respectively) and its relationship with protein and isoflavone composition before and after in vitro gastrointestinal digestion and absorption. Anti-inflammatory activity of GC digests was almost 2-fold higher than CC digests (p < 0.05), which was associated to greater content of peptides, formononetin and biochanin A (p < 0.05). Anti-inflammatory activity of phenolic fraction in digests was 7-fold higher than the protein fraction (p < 0.05). The most active peptide fraction from GC digest (IC = 93 µg/mL) contained a total of 24 peptides derived from legumin and vicilin. In conclusion, this study stands out the potential of germinated chickpea proteins concentrates to exert anti-inflammatory effects in the lower gut which may contribute to the prevention of bowel inflammatory diseases.

Enzymatic Production, Bioactivity, and Bitterness of Chickpea (Cicer arietinum) Peptides

“…Globally, the Codex Alimentarius provides general guidelines on the use of enzymes as processing aids, whereas in the United States, volume 3 chapter 1 of Title 21 in the Code of Federal Regulations specifies approved enzymes for use in food products (Codex Alimentarius Comission, ; U.S. Food and Drug Administration, ). Chickpea peptides have been reported to have been produced by the enzymes alcalase, α‐chymotrypsin, flavorzyme, papain, pepsin, and trypsin either alone or in combination during the past 20 years (Barbana & Boye, ; del Mar Yust et al., ; Girón‐Calle, Alaiz, & Vioque, ; Kou, Gao, Zhang, Wang, & Wang, ; Milán‐Noris, Gutiérrez‐Uribe, Santacruz, Serna‐Saldívar, & Martínez‐Villaluenga, ; Pedroche et al., ; Torres‐Fuentes, Alaiz, & Vioque, ; Yust et al., ).…”

“…There is currently no distinct pattern to the sequenced chickpea peptides produced by pepsin followed by pancreatin digestion across studies, with sequenced peptides reported by Milán‐Noris et al. () mainly having a terminal lysine residue, whereas those reported by Torres‐Fuentes et al. () mainly have a terminal leucine residue.…”

“…Although analyzing peptides formed through pepsin–pancreatin digestion might provide valuable information about the types of peptides that a protein sample might naturally produce upon digestion, it may not provide information about novel peptides that would not naturally be produced by the body. Chickpea protein hydrolysates and peptides formed through simulated gastrointestinal digestion have mainly shown antioxidant, ACE inhibitory, anti‐inflammatory, and anticarcinogenic bioactivities (Barbana & Boye, ; Jamdar, Deshpande, & Marathe, ; Milán‐Noris et al., ; Sánchez‐Chino et al., ). Although chickpea proteins might be able to naturally produce health promoting peptides during digestion, chickpea storage proteins have been found to resist gastrointestinal digestion, so the quantity of peptides produced from these proteins might be lower in reality than what has been measured in in vitro systems (Wang et al., ).…”

“…Food and Drug Administration, 2018). Chickpea peptides have been reported to have been produced by the enzymes alcalase, α-chymotrypsin, flavorzyme, papain, pepsin, and trypsin either alone or in combination during the past 20 years (Barbana & Boye, 2010;del Mar Yust et al, 2012;Girón-Calle, Alaiz, & Vioque, 2010;Kou, Gao, Zhang, Wang, & Wang, 2013;Milán-Noris, Gutiérrez-Uribe, Santacruz, Serna-Saldívar, & Martínez-Villaluenga, 2018;Pedroche et al, 2002;Torres-Fuentes, Alaiz, & Vioque, 2011;Yust et al, 2003).…”

“…hydrolysis due to alcalase (Table 4). There is currently no distinct pattern to the sequenced chickpea peptides produced by pepsin followed by pancreatin digestion across studies, with sequenced peptides reported by Milán-Noris et al (2018) mainly having a terminal lysine residue, whereas those reported by Torres-Fuentes et al (2015) mainly have a terminal leucine residue. Only small peptides composed of five amino acids or less have been sequenced from those produced by alcalase hydrolysis of chickpea proteins (Table 4).…”