Effect of chickpea protein hydrolysates on cell proliferation and in vitro bioavailability

Girón‐Calle, Julio; Alaiz, Manuel; Vioque, Javier

doi:10.1016/j.foodres.2010.03.020

Cited by 64 publications

(50 citation statements)

References 41 publications

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“…Publications evidencing pulse hydrolysates or BPs active toward cancer or related syndromes have recently appeared. Girón‐Calle and others () evaluated cancer cell proliferation after treatment with hydrolysates from chickpea digested with pepsin/pancreatin. Hydrolysates <3 kDa inhibited human epithelial colorectal adenocarcinoma cells (Caco‐2) and monocytics leukemia cells (THP‐1) up to 48% and 78%, respectively.…”

Section: Cancer Preventingmentioning

confidence: 99%

Bioactive Peptides and Hydrolysates from Pulses and Their Potential Use as Functional Ingredients

López-Barrios

Gutiérrez-Uribe

Serna‐Saldívar

2014

Journal of Food Science

149

100

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Abstract:Bioactive peptides (BPs) are amino acid sequences derived from food proteins. Their relevance lies in the biological activities they have once they are released from the parent protein. BPs or protein hydrolysates can be commercialized as nutraceutical products or functional ingredients according to their activities. Different food protein sources have been researched for their potential to generate BPs. However, with the exception of lunasin (derived from soy), animal protein sources have been predominantly exploited as commercial BPs sources. On the other hand, pulses have shown diverse BP contents without further impact on their commercialization. Pulses are a rich source of protein in the human diet and their consumption has been associated with the prevention of chronic diseases. The beneficial effect in human health has been related to their micronutrients, phytochemical bioactive compounds, and recently BPs. This article reviews the current literature about pulse protein hydrolysates and BPs with proved angiotensin converting enzyme inhibitory, antioxidant, cancer preventing, and other health promoting activities. Proteolysis process is commonly achieved by digestive and microorganism enzymes. BP purification and identification has consisted mainly on size segregation procedures followed by mass spectrometry techniques. Hydrolysis time, peptide size, and hydrophobicity are employed as process variants and structural features relevant for the BP activities. Finally, some considerations about industrial processing and BPs used as functional food ingredients were reviewed.

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Section: Cancer Preventingmentioning

confidence: 99%

Bioactive Peptides and Hydrolysates from Pulses and Their Potential Use as Functional Ingredients

López-Barrios

Gutiérrez-Uribe

Serna‐Saldívar

2014

Journal of Food Science

149

100

View full text Add to dashboard Cite

show abstract

“…For instance, many studies reported the presence of anti-hypertensive [1][2][3][4], opioid [5,6] and antimicrobial [7][8][9] peptides in various protein hydrolysates. Furthermore, a growth-promoting [10][11][12] or growthinhibiting [13] effect in cell cultures has been reported for some protein hydrolysates. Various additional functionalities and bioactivities have been described [9,14], and the literature on this subject is expanding.…”

Section: Introductionmentioning

confidence: 95%

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

et al. 2012

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A new method to predict elementary amino acid (AA) composition of peptides (molar mass <1,000 g/mol) is described. This procedure is based on a computer-aided method using three combined analyses-reversed phase liquid chromatography (RPLC), hydrophilic interaction chromatography (HILIC) and capillary electrophoresis coupled with mass spectrometry-and using a software calculating all possible amino acid combinations from the mass of any given peptide. The complementarity between HILIC and RPLC was demonstrated. Peptide retention prediction in HILIC was successfully modelled, and the achieved prediction accuracy was as high as r²=0.97. This mathematical model, based on amino acid retention contributions and peptide length, provided the information about peptide hydrophilicity that was not redundant with its hydrophobicity. Correlations between respectively the hydrophobicity coefficients and RPLC retention time, hydrophilicity and HILIC retention time, and electrophoretic mobility and migration time were used for ranking all potential AA combinations corresponding to the given mass. The essential contribution of HILIC in this identification strategy and the need to combine the three models to significantly increase identification capabilities were both shown. Applied to an 18-standard peptide mixture, the identification procedure enabled the actual AA combination determination of the 14 di- to pentapeptides, in addition to an over 98 % reduction of possible combination numbers for the four hexapeptides. This procedure was then applied to the identification of 24 unknown peptides in a rapeseed protein hydrolysate. The effective AA composition was found for ten peptides, whereas for the 14 other peptides, the number of possible combinations was reduced by over 95 % thanks to the association of the three analyses. Finally, as a result of the information provided by the analytical techniques about peptides present in the mixture, the proposed method could become a highly valuable tool to recover bioactive peptides from undefined protein hydrolysates.

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“…In recent years, in vitro hydrolysis of proteins has led to the discovery of numerous anticancer hydrolysates (Alemán et al, 2011;Girón-Calle, Alaiz, & Vioque, 2010;Kannan, Hettiarachchy, Johnson, & Nannapaneni, 2008;Kops, West, Leach, & Miller, 1997;Picot et al, 2006). Furthermore, several anticancer or antiproliferative peptides were purified from marine derived protein hydrolysates.…”

Section: Introductionmentioning

confidence: 99%

Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

Song

Wei

Luo

et al. 2014

Journal of Functional Foods

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Effect of chickpea protein hydrolysates on cell proliferation and in vitro bioavailability

Cited by 64 publications

References 41 publications

Bioactive Peptides and Hydrolysates from Pulses and Their Potential Use as Functional Ingredients

Bioactive Peptides and Hydrolysates from Pulses and Their Potential Use as Functional Ingredients

Hydrophilic properties as a new contribution for computer-aided identification of short peptides in complex mixtures

Isolation and identification of an antiproliferative peptide derived from heated products of peptic hydrolysates of half-fin anchovy (Setipinna taty)

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