Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties

Nongonierma, Alice B.; Maux, Solène Le; Dubrulle, Cécile; Barre, Chloé; Fitzgerald, Richard J.

doi:10.1016/j.jcs.2015.07.004

Cited by 124 publications

(92 citation statements)

References 27 publications

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“…Quinoa attracts increasing interest, because of its high-protein content (9.1-15.7 g) and gluten-free (Nowak, Du, & Charrondi ere, 2016). Quinoa protein hydrolyzates produced by papain showed the dipeptidyl peptidase IV inhibitory and oxygen radical absorbance capacity activities (Nongonierma, Maux, Dubrulle, Barre, & Fitzgerald, 2015). Recently, the protein from Quinoa has also been accepted as source of bioactive peptides.…”

Section: Introductionmentioning

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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Section: Introductionmentioning

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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“…The extraction yield and the purity of the -La obtained were calculated as described elsewhere 12 .…”

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confidence: 99%

“…The -La content of the isolate was determined by reverse-phase high-performance liquid chromatography (RP-HPLC) as described by Nongonierma and FitzGerald 11 , using an -La standard sample (Sigma-Aldrich). The extraction yield and the purity of the -La obtained were calculated as described elsewhere 12 .…”

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confidence: 99%

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

et al. 2016

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Bovine α-lactalbumin (α-La) contains numerous dipeptidyl peptidase IV (DPP-IV) inhibitory peptides sequences within its primary structure. In silico analysis indicated that the targeted hydrolysis of α-La with elastase should release DPP-IV inhibitory peptide sequences. An α-La isolate was hydrolysed with elastase under different conditions using an experimental design approach incorporating 3 factors (temperature, pH and enzyme to substrate ratio (E:S) ratio) at 2 levels. The hydrolyzate generated at pH 8.5, 50C, E:S 2.0% (w/w) (H9) displayed the lowest half maximal DPP-IV inhibitory concentration (IC50 = 1.20 ± 0.12 mg mL -1). Five α-La-derived DPP-IV inhibitory peptides (GY, GL, GI, NY and WL) predicted to be released in silico were identified by liquid-chromatography tandem mass spectrometry (LC-MS/MS) within H9 and its simulated gastrointestinal digestion (SGID) sample. This proof of concept study demonstrated the benefit of using a targeted approach combined with an experimental design in the generation of dietary protein hydrolyzates with DPP-IV inhibitory properties. IntroductionDipeptidyl peptidase IV (DPP-IV) is an ubiquitous enzyme which is responsible for the cleavage and inactivation of the incretin hormones, glucose dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) 1 . In the context of type 2 diabetes management, DPP-IV inhibition may be used as a means to improve the regulation of serum glucose in humans. Various DPP-IV inhibitory drugs (gliptins), have been developed to maintain the insulinotropic activity of the incretins in the post-prandial phase 2 .Dietary components, including food protein-derived peptides, have been shown to play a role in the inhibition of DPP-IV in vitro and in certain instances in vivo, for reviews, see: 3,4,5 . In silico studies have shown that selected DPP-IV inhibitory peptide sequences may be found within a wide range of dietary proteins 6,7 . To date, milk proteins appear to be the most frequently studied substrate for the generation of DPP-IV inhibitory peptides. Depending on the enzymatic strategy employed, different milk proteins may appear to be more suitable substrates for the production of DPP-IV inhibitory peptides. For instance, it was recently predicted by Tulipano et al.8 using in silico digestion with gastrointestinal proteinases that -lactoglobulin (-Lg) should yield a higher number of previously identified DPP-IV inhibitory peptides than -La. This was further confirmed following in vitro digestion of -Lg and -La with gastrointestinal enzymes, yielding hydrolyzates with IC 50 values of 0.74 and 1.70 mg mL -1, respectively 8 . Other in silico analysis of the major milk proteins indicated that -lactalbumin (-La) displayed the highest level of sequence coverage (43.9%) for previously identified DPP-IV inhibitory peptides as well as the highest DPP-IV inhibitory potency index (i.e., 17.9 10 -6 µM -1 g -1 ) 7 . It has been suggested that discrepancies between studies to determine the most adequate substrate for the genera...

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“…However, as emerging vegetable proteins include pumpkin seeds (Cucurbita maxima), ahuyama (Cucurbita moschata), quinoa (Chenopodium quinoa) and chia (Hispanic Salvia), and legumes such as black bean (Phaseolus Vulgaris), lentils (Lens culinaris), peas (Pisumsativum) and chickpeas (Cicer arietinum). All these sources are considered as vegetable sources that have a high protein content, ranging from 24% to 36%, 25% to 30%, 12% to 23%, 17% to 22%, 22% to 26%, 12% to 23% , 10% to 18% and 15% to 25%, respectively (Quanhong and Caili, 2005;Aluko et al, 2015 Nongonierma et al, 2015;Shevkani et al, 2015;Torresfuentes et al, 2015;Wang et al, 2015;Xu et al, 2016).…”

Section: Cationization Reactionmentioning

confidence: 99%

“…Moreover, the antioxidant activity and nutritional content of some peptides modified by chemical and enzymatic hydrolyses, have been evaluated assessing the contribution of essential amino acids on those properties (Quanhong and Caili, 2005;Aluko et al, 2015;Ariyarathna and Karunaratne, 2015;Bucko et al, 2015;Nongonierma et al, 2015;Shevkani et al, 2015;Torresfuentes et al, 2015;Wang et al, 2015;Xu et al, 2016). This opens a door of opportunities to study the functional properties and encapsulation capacity of different vegetable sources of proteins.…”

Section: Cationization Reactionmentioning

confidence: 99%

Wheatgrass juice, Sensory analyses, Novel food, Functional food

Quiroz¹,

Rojas²,

Ciro-Gómez³

2018

Food Res.

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Proteins from plant sources are macromolecules of industrial interest due to its high availability, biodegradability, renewable character and functional properties such as biocompatibility, good amphiphilic properties, water solubility, foaming, emulsifying, gelling and film-forming abilities. In this scenario, these macromolecules have a high applicability in various emulsification stabilization processes, and have a potential use as a wall-forming material for the encapsulation processes of active ingredients. Currently, proteins extracted from soybean, pea, sunflower, rice and wheat seeds have already been studied as versatile stabilizers and emulsion coatings by coacervation and encapsulation processes by spray-drying. However, the capsule-forming ability of these macromolecules is enhanced by physical, chemical or enzymatic changes in their structure, favoring the interactions with the core material, the solvent, and increase of the encapsulation efficiency and its versatility in other encapsulation techniques.

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Quinoa (Chenopodium quinoa Willd.) protein hydrolysates with in vitro dipeptidyl peptidase IV (DPP-IV) inhibitory and antioxidant properties

Cited by 124 publications

References 27 publications

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

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

Strategies for the release of dipeptidyl peptidase IV (DPP-IV) inhibitory peptides in an enzymatic hydrolyzate of α-lactalbumin

Wheatgrass juice, Sensory analyses, Novel food, Functional food

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