Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate

Ghribi, Abir Mokni; Gafsi, Ines Maklouf; Sila, Assaâd; Blecker, Christophe; Danthine, Sabine; Attia, Hamadi; Bougatef, Ali; Besbes, Souhail

doi:10.1016/j.foodchem.2015.04.109

Cited by 227 publications

(81 citation statements)

References 31 publications

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“…This endopeptidase enzyme could influence the quaternary and tertiary conformations of proteins by cleaving peptide bonds within individual or aggregated proteins to produce smaller protein sub-units and/or smaller peptides. [14] Glycosylation could produce Maillard reaction products (MRPs) of hydrolyzed OVA, which were between 20.1 kDa and 29 kDa. It has been widely demonstrated that these MRPS provide better emulsifying capability, heat stability, foaming, solubility, as well as reduce allergenicity compared to native protein.…”

Section: Resultsmentioning

confidence: 99%

“…[13] Limited enzymatic hydrolysis could reduce molecular weight, but exposured hydrophobic groups previously buried in the protein, [14][15][16] which might increase the protein foaming capacity and emulsifying properties. However, to the best of our knowledge, most papers have been reported to use enzymatic hydrolysis to produce EWP peptides [17][18][19] or reduce its allergenicity, [11] few reports about using enzymatic hydrolysis to improve the functional properties of EWP.…”

Section: Introductionmentioning

confidence: 99%

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Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Liu

Prakash

et al. 2018

International Journal of Food Properties

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The functional and structural properties of enzymatic hydrolysis and glycosylation synergistic modified ovalbumin (OVA) were investigated. The results showed that hydrolysis and glycosylation had synergetic effects on emulsifying and foaming properties, water and oil-binding capacity of OVA. And hydrolysis and glycosylation also could improve gel strength and thermal properties of OVA. Polyacrylamide gel electrophoresis analysis implied that the formation of 20.1 kDa~29 kDa Maillard reaction products (MRPs). UV absorption and Fourier Transform Infrared spectroscopy analyses confirmed that enzymatic hydrolysis and glycosylation could change the secondary structure of OVA. Moreover, hydrolysis and glycosylation could produce OVA with compact and orderly network structure.

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Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Liu

Prakash

et al. 2018

International Journal of Food Properties

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“…1.B 15 were surface-active. Furthermore, Mokni Ghribi et al [29] confirmed that the increase in the DH value led to a reduction in the surface activity by a decrease in the first drop value. This can be explained by the fact that hydrolysis leads to the release of small peptides into solution.These small peptides, with the same charge, presented antagonist behaviour and can compete to reach the air-water interface, which ultimately results in the slow diffusion into interface.…”

Section: Aqueous Suspensions Properties: Surface Tension Measurementsmentioning

confidence: 91%

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Krichen

Sila

Caron

et al. 2018

Engineering in Life Sciences

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The effect of enzymatic hydrolysis by Savinase on the interfacial properties and antihypertensive activity of shrimp waste proteins was evaluated. The physicochemical characterization, interfacial tension, and surface characteristics of shrimp waste protein hydrolysates (SWPH) using different enzyme/substrate (E/S) (SWPH5 (SWPH using E/S = 5), SWPH15 (SWPH using E/S = 15), and SWPH40 (SWPH using E/S = 40)) were also studied. SWPH5, SWPH15, and SWPH40 had an isoelectric pH around 2.07, 2.17, and 2.54 respectively. SWPH5 exhibited the lowest interfacial tension (68.96 mN/m) followed by SWPH15 (69.36 mN/m) and SWPH40 (70.29 mN/m). The in vitro ACE inhibitory activity of shrimp waste protein hydrolysates showed that the most active hydrolysate was obtained using an enzyme/substrate of 15 U/mg (SWPH15). SWPH15 had a lower IC50 value (2.17 mg/mL) than that of SWPH5 and SWPH40 (3.65 and 5.7 mg/mL, respectively). This hydrolysate was then purified and characterized. Fraction F1 separated by Sephadex G25 column which presents the best ACE inhibition activity was then separated by reversed‐phase high performance liquid chromatography. Four ACE inhibitory peptides were identified and their molecular masses and amino acid sequences were determined using ESI–MS and ESI–MS/MS, respectively. The structures of the most potent peptides were SSSKAKKMP, HGEGGRSTHE, WLGHGGRPDHE, and WRMDIDGDIMISEQEAHQR. The structural modeling of anti‐ACE peptides from shrimp waste through docking simulations results showed that these peptides bound to ACE with high affinity.

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“…For instance, alcalase was used to prepare hydrolyzate from peanut protein, chickpea protein, rice protein, and hemp seed protein (Ghribi et al, 2015;Jamdar et al, 2010;Ren et al, 2016;Xue, Li, et al, 2017). For instance, alcalase was used to prepare hydrolyzate from peanut protein, chickpea protein, rice protein, and hemp seed protein (Ghribi et al, 2015;Jamdar et al, 2010;Ren et al, 2016;Xue, Li, et al, 2017).…”

Section: Enzymatic Hydrolysis Of Pretreated Qpimentioning

confidence: 99%

Effects of high‐intensity ultrasound pretreatment with different levels of power output on the antioxidant properties of alcalase hydrolyzates from Quinoa (Chenopodium quinoa Willd.) protein isolate

et al. 2018

Cereal Chem

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Background and objectives:The effects of ultrasound pretreatment with different levels of power output (200, 400, and 600 W) on hydrolysis degree of Quinoa protein isolate (QPI) and antioxidant activity of QPI hydrolyzate were studied.The secondary structure, surface hydrophobicity, intrinsic fluorescence, and scanning electron microscopy (SEM) of QPI treated by ultrasound were measured.The untreated QPI and high-temperature treatment (90°C for 30 min) were used as control. Findings:The results showed that ultrasound pretreatment at 400 W significantly improved the hydrolysis degree of QPI and antioxidant activity of QPI hydrolyzate. The changes in secondary structure, surface hydrophobicity, and intrinsic fluorescence indicated the unfolding of QPI after ultrasound. The SEM results showed that ultrasound treatment resulted in the deformation of QPI. Conclusions:The improvement in degree of hydrolysis might be related to the changes in structure induced by ultrasound treatment, which supported more groups for the process of enzymatic hydrolysis. Significance and novelty: The power output selection of ultrasound pretreatment is essential for improvement of accessibility of QPI to the alcalase and preparation of antioxidant peptides. K E Y W O R D Santioxidant activity, Quinoa protein isolate, structure, ultrasound pretreatment

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Effects of enzymatic hydrolysis on conformational and functional properties of chickpea protein isolate

Cited by 227 publications

References 31 publications

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Enzymolysis and glycosylation synergistic modified ovalbumin: functional and structural characteristics

Identification and molecular docking of novel ACE inhibitory peptides from protein hydrolysates of shrimp waste

Effects of high‐intensity ultrasound pretreatment with different levels of power output on the antioxidant properties of alcalase hydrolyzates from Quinoa (Chenopodium quinoa Willd.) protein isolate

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