Combined effects of high-pressure and enzymatic treatments on the hydrolysis of chickpea protein isolates and antioxidant activity of the hydrolysates

Zhang, Tao; Jiang, Bo; Miao, Ming; Mu, Wanmeng; Li, Yanhong

doi:10.1016/j.foodchem.2012.05.097

Cited by 75 publications

(43 citation statements)

References 36 publications

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“…As compared to the proteolysis at atmospheric pressure, proteolysis under HP led to qualitative differences in the hydrolysis pattern observed by SDS-PAGE, except for Alcalase (Figure 1 Figure 1B). This observation is consistent with a previous study showing that Alcalase activity increased slightly at low pressure levels (100-300 MPa) (Zhang et al, 2012). In contrast, pressurisation above 200 MPa considerably increased lentil proteins susceptibility to enzymatic hydrolysis by Savinase, Protamex and Corolase (Figure 1, panel A).…”

Section: Effect Of Pressurisation On Enzymatic Hydrolysis Of Lentil Psupporting

confidence: 92%

“…HP offers the food industry applications in food preservation and creation of novel foods, textures and tastes. Besides these major applications, HP has also been used in combination with protease treatments for the production of hypoallergenic (Peñas, Restani, Ballabio, Préstamo, Fiocchi, & Gomez, 2006;López-Expósito, Chicón, Belloque, Recio, Alonso, & López-Fandiño, 2008) and functional hydrolysates containing bioactive peptides (Hoppe, Jung, Patnaik, & Zeece, 2013;Zhang, Jiang, Miao, Mu, & Li, 2012). Previous studies have demonstrated that enzymatic proteolysis under high pressure conditions enhances the protein susceptibility to digestion (Chicón et al, 2006;Quirós, Chicón, Recio, & López-Fandiño, 2007) which makes this technology worthy of consideration to increase hydrolytic products yields and to reduce reaction time and production costs.…”

Section: Introductionmentioning

confidence: 99%

“…The literature about the application of high-pressure assisted proteolysis in the production of bioactive peptides from legume proteins has been largely unexplored. There is only one recent study showing that high pressure pre-treatment of chickpea proteins reduces hydrolysis time and enhance the formation of antioxidant peptides in the hydrolysates (Zhang et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins

et al. 2015

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Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention due to their beneficial effects in the prevention/treatment of hypertension. The objective was to explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the release of bioactive peptides from lentil proteins. Pressurisation (100-300 MPa) enhanced the hydrolytic efficiency of Protamex, Savinase and Corolase 7089 compared to Alcalase. Proteolysis at 300 MPa led to a complete degradation of lentil proteins and increased peptide (<3 kDa) concentration by all enzymes. Proteolysis at 300 MPa by Savinase gave rise to lentil hydrolysates (S300) with the highest ACE-inhibitory and antioxidant activities that were retained upon in vitro gastrointestinal digestion. The peptides responsible for the multifunctional properties of S300 hydrolysate were identified as different fragments from storage proteins and the allergen Len c 1. These results support the potential of HP as a technology for the cost-effective production of bioactive peptides from lentil proteins during enzymatic proteolysis.

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Section: Effect Of Pressurisation On Enzymatic Hydrolysis Of Lentil Psupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins

et al. 2015

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“…The absorbance values for both of these samples were slightly reduced (0.5) in comparison to samples processed at 300 MPa indicating the complete denaturation stage of almond proteins. Zhang et al 48 has also reported such structural information related with alteration of protein structure at high pressure in chickpea protein isolate solutions. (72 ∘ C) ( Fig.…”

Section: Uv Absorption Spectra Of Pressure-treated Almond Milkmentioning

confidence: 98%

Effect of high pressure processing on dispersive and aggregative properties of almond milk

2016

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“…Alcalase has been widely used in the production of chickpea protein hydrolysates and peptides. Chickpea protein hydrolysates formed by alcalase alone have been shown to have potential antioxidant, ACE inhibitory, and hypolipidemic bioactives (Medina-Godoy et al, 2012;Shi, Hou, Liu, Guo, & He, 2019;Zhang, Jiang, Miao, Mu, & Li, 2012). Alcalase was used to hydrolyze chickpea protein isolate to produce the peptide NRYHE, whose antioxidant activity has been well studied in both chemical and cellular models (Guo, Zhang, Jiang, Miao, & Mu, 2014;Zhang, Li, Miao, & Jiang, 2011).…”

Section: Microbial Proteases (Alcalase and Flavorzyme)mentioning

confidence: 99%

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

Hernandez

Mejía

2019

Comp Rev Food Sci Food Safe

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Chickpeas are inexpensive, protein rich (approximately 20% dry mass) pulses available worldwide whose consumption has been correlated with positive health outcomes. Dietary peptides are important molecules derived from dietary proteins, but a comprehensive analysis of the peptides that can be produced from chickpea proteins is missing in the literature. This review provides information from the past 20 years on the enzymatic production of peptides from chickpea proteins, the reported bioactivities of chickpea protein hydrolysates and peptides, and the potential bitterness of chickpea peptides in food products. Chickpea peptides have been enzymatically produced with pepsin, trypsin, chymotrypsin, alcalase, flavorzyme, and papain either alone or in combination, but the sequences of many of the peptides in chickpea protein hydrolysates remain unknown. In addition, a theoretical hydrolysis of chickpea legumin by stem bromelain and ficin was performed by the authors to highlight the potential use of these enzymes to produce bioactive chickpea peptides. Antioxidant activity, hypocholesterolemic, and angiotensin 1‐converting enzyme inhibition are the most studied bioactivities of chickpea protein hydrolysates and peptides, but anticarcinogenic, antimicrobial, and anti‐inflammatory effects have also been reported for chickpea protein hydrolysates and peptides. Chickpea bioactive peptides are not currently commercialized, but their bitterness could be a major impediment to their incorporation in food products. Use of flavorzyme in the production of chickpea protein hydrolysates has been proposed to decrease their bitterness. Future research should focus on the optimization of chickpea bioactive peptide enzymatic production, studying the bioactivity of chickpea peptides in humans, and systematically analyzing chickpea peptide bitterness.

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Combined effects of high-pressure and enzymatic treatments on the hydrolysis of chickpea protein isolates and antioxidant activity of the hydrolysates

Cited by 75 publications

References 36 publications

High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins

High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins

Effect of high pressure processing on dispersive and aggregative properties of almond milk

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

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