Purification and identification of novel antioxidant peptides from enzymatic hydrolysate of chickpea (Cicer arietinum L.) protein concentrate

Ghribi, Abir Mokni; Sila, Assaâd; Przybylski, Rémi; Nedjar‐Arroume, Naïma; Makhlouf, Ines; Blecker, Christophe; Attia, Hamadi; Dhulster, Pascal; Bougatef, Ali; Besbes, Souhail

doi:10.1016/j.jff.2014.12.011

Cited by 102 publications

(73 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…At present, bran protein (Thamnarathip, Jangchud, Nitisinprasert, & Vardhanabhuti, ), cod protein ( Gadus morhua ) (Girgih et al, ), chickpea ( Cicer arietinum L .) (Ghribi et al, ), bluefin leatherjacket protein (Chi, Wang, Wang, Zhang, & Deng, ), oil palm kernel protein (Chang, Ismail, Yanagita, Mohd Esa, & Baharuldin, ), oysters ( Crassostrea talienwhanensis ) (Wang et al, ), chicken skin protein (Onuh, Girgih, Aluko, & Aliani, ), and round scad muscle protein (Jiang et al, ) have been confirmed to have antioxidative activities. Moreover, the above‐mentioned hydrolyzed peptides showed potent radical scavenging activity among their experiments.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant activity of queen bee larvae processed by enzymatic hydrolysis

Deyuan

Dong

Liu

et al. 2017

J Food Process Preserv

View full text Add to dashboard Cite

Queen bee larvae (QBL), by‐products of royal jelly processing, was enzymatically hydrolyzed to produce bioactive peptides. Five enzymes were firstly used to obtain hydrolysates which were evaluated for their antioxidative performances. QBL hydrolyzed by pepsin, showing the highest antioxidant resistance, were prepared and isolated by ultrafiltration using different molecular weight cutoffs of <1, 1–5, 5–10, and >10 kDa. Then, hydrolysate III (MW 1–5 kDa) with the highest activity was purified through continuous chromatography. Antioxidant capacities of active peak 3 (P3) to DPPH, hydroxyl, superoxide, ABTS, oxygen radical absorbance capacity radicals assay were 74.31%, 82.44%, 74.53%, 78.81%, and 1,074 μM TE/g, respectively. Finally, the most potent antioxidant hydrolysate was determined through a high‐speed amino acid analyzer. The results of the QBLH for in vitro antioxidant assays have indicated that P3 is a good antioxidative peptide due to its high percentage of hydrophobic amino acids and has vast prospects for future development and application. Practical applications QBL has been used as a traditional medicine for several millennia in China due to its rich nutrition and potent effect in improving human immunity, however, the utilization of QBL resources industry is rather low. This article evaluated the antioxidant activities of queen bee larvae using DPPH, hydroxyl, superoxide, ABTS, ORAC radicals assay, respectively. This article indicates that high antioxidant amino acid residues can be obtained from QBL through simple processing methods (enzymatic hydrolyzing and membrane isolating). Our study could arouse a great interest among researchers to develop a new series of QBL products with high efficient antioxidant properties.

show abstract

Section: Introductionmentioning

confidence: 99%

Antioxidant activity of queen bee larvae processed by enzymatic hydrolysis

Deyuan

Dong

Liu

et al. 2017

J Food Process Preserv

View full text Add to dashboard Cite

show abstract

“…Recently, proteins and their hydrolysates have drawn research interest due to their wide distribution, low toxicity, excellent free radical scavenging activity and metal ion-binding ability (Moure et al, 2006;Pownall et al, 2010). Plant sources, such as cherry seed (Garc ıa et al, 2015), alfalfa leaf (Xie et al, 2008) and chickpea (Ghribi et al, 2015), have been used to investigate the antioxidant activities of proteins and enzymatic hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Effects of simulated gastrointestinal digestion on the physicochemical properties, erythrocyte haemolysis inhibitory ability and chemical antioxidant activity of mulberry leaf protein and its hydrolysates

Sun

Yin

et al. 2017

Int J of Food Sci Tech

View full text Add to dashboard Cite

Summary Proteins and peptides must be degraded and modified in the gastrointestinal (GI) tract prior to absorption; this process changes their physicochemical and biological properties. Mulberry leaf protein (MP) and its hydrolysates (HMP) have favourable antioxidant activities. To investigate, in vitro and separately, the effects of GI digestion and intestinal digestion on the stability of MP and HMP, we monitored the changes in secondary structures, amino acids, molecular weights and antioxidant activities. We found that MP was more hydrolysed by pepsin than by pancreatin, unlike HMP. The final digests of MP and HMP were mainly composed of polypeptides (0.5–6.5 kDa) and oligopeptides (<0.5 kDa), respectively. The GI digestion influenced MP and HMP differently; GI digestion increased the antioxidant efficiency of MP and decreased that of HMP. For the intestinal digests, the antioxidant activities of MP and HMP also differed. The 1,1‐diphenyl‐2‐picrylhydrazyl (DPPH) and 2,2′‐azinobis (3‐ethylbenzothiazoline‐6‐sulphonic acid) diammonium salt (ABTS) radical quenching abilities of MP and HMP at 1 mg mL−1 were comparable to or exceeded that of L‐glutathione (GSH) and 6‐hydroxy‐2,5,7,8‐tetramethychroman‐2‐carboxylic acid (trolox). Meanwhile, the erythrocyte haemolysis rates of MP, HMP and their GI products at 0.05–1.0 mg mL−1 were significantly lower than that of the 2,2′‐azobis (isobutyramidine) dihydrochloride (AAPH) control. Both MP and HMP can be used as natural antioxidants and may promote digestive health.

show abstract

“…Nevertheless, if not absorbed, these peptides can locally exert their function. This is the reason why the finding of antioxidant peptides derived from plant materials, such as peanut (Ji, Sun, Zhao, & Sun, 2014), amaranth (Orsini Delgado et al, 2016), chickpea (Ghribi et al, 2015), walnut (Gu et al, 2015), and corn (Jin, Liu, Zheng, Wang, & He, 2016), has been recently intensified.…”

mentioning

confidence: 99%

Fractionation and characterization of antioxidant peptides from rice bran protein hydrolysates stimulated by in vitro gastrointestinal digestion

Phongthai

Rawdkuen

2020

Cereal Chem

View full text Add to dashboard Cite

Background and objective Rice bran protein concentrate was prepared and hydrolyzed by using pepsin–pancreatin. The obtained result was further filtered through 5‐kDa membranes. A permeate was collected and sequentially fractionated by different chromatographic techniques. The peptide fractions were determined for the antioxidant activities. Findings Three peptide fractions were derived after separating the crude protein hydrolysates by anion‐exchange chromatography. Due to its highest ABTS radical scavenging and metal chelating activities (p < .05), fraction F2‐A was pooled and separated further by size‐exclusion chromatography (SEC). Among the SEC fractions, F1‐S showed strongest antioxidant activities; thus, it was collected for reverse‐phase HPLC purification. Subsequently, the peptide fractions were successfully separated and F4‐H had the greatest ABTS‐scavenging activities (214.61 µmol Trolox/g sample, respectively). In addition, it displayed the strongest ability to reduce ferric to ferrous ions (104.80 µmol FeSO4/g sample) (p < .05), while F1‐H showed the highest ability to chelate metal ions (266.40 µmol EDTA/g sample) (p < .05). Conclusion These results demonstrate that hydrophobic amino acids play a major role in scavenging free radicals, whereas polar amino acids are responsible for reducing and chelating metal ions. Significance and novelty Rice bran protein composes of high ratio of hydrophobic amino acid. It is a suitable source of antioxidant peptides that might be produced during gastrointestinal digestion. Separation and purification using chromatographic techniques showed promising results for selectively fractionate antioxidant peptides with specific activity.

show abstract

Purification and identification of novel antioxidant peptides from enzymatic hydrolysate of chickpea (Cicer arietinum L.) protein concentrate

Cited by 102 publications

References 39 publications

Antioxidant activity of queen bee larvae processed by enzymatic hydrolysis

Antioxidant activity of queen bee larvae processed by enzymatic hydrolysis

Effects of simulated gastrointestinal digestion on the physicochemical properties, erythrocyte haemolysis inhibitory ability and chemical antioxidant activity of mulberry leaf protein and its hydrolysates

Fractionation and characterization of antioxidant peptides from rice bran protein hydrolysates stimulated by in vitro gastrointestinal digestion

Contact Info

Product

Resources

About