Effect of enzymatic hydrolysis using endo- and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates

Xu, Yixiang; Galanopoulos, Magdalini; Sismour, Edward; Ren, Shuxin; Mersha, Zelalem; Lynch, Patricia A.; Almutaimi, Abeer

doi:10.1007/s11694-019-00296-0

Cited by 66 publications

(73 citation statements)

References 39 publications

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“…After 90 min, the DH of the chickpea genotypes varied significantly ( p < 0.05) from 40.2% to 45.1% in the globulin extracts and from 32.1% to 41.4% in the albumin extracts (Table 1). These values correspond with those reported previously in chickpea protein extracts treated with alcalase (Kou et al., 2013; Xu et al., 2020).…”

Section: Resultssupporting

confidence: 92%

“…Alcalase is an inexpensive endopeptidase with a broad catalytic activity and has been widely used to produce protein hydrolyzates and bioactive peptides in legumes, including chickpea (Ghribi et al., 2015; Kou et al., 2013; Xu et al., 2020). The hydrolysis curves of the globulin and albumin protein extracts treated with alcalase showed a high rate of hydrolysis during the first 30–40 min (Figure S1).…”

Section: Resultsmentioning

confidence: 99%

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Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates

Quintero‐Soto

Chávez-Ontiveros

Garzón‐Tiznado

et al. 2021

Journal of Food Science

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Alcalase hydrolyzates were prepared from the albumin (AH) and globulin (GH) fractions of eight chickpea (Cicer arietinum L.) genotypes from Mexico and 10 from other countries. Protein content, antioxidant activity (AA) (ABTS, DPPH), and degree of hydrolysis were evaluated and the best genotype was selected by principal component analysis. The hydrolyzates of the chosen genotype were analyzed for its antidiabetic potential measured as inhibition of α‐amylase, α‐glucosidase, and dipeptidyl peptidase‐4 (DPP4). Peptide profiles were obtained by liquid chromatography‐mass spectrometry (UPLC‐DAD‐MS), and the most active peptides were analyzed by molecular docking. The average antioxidant activity of albumin hydrolyzates was higher than that of globulin hydrolyzates. ICC3761 was the selected genotype and peptides purified from the albumin hydrolyzate showed the best antioxidant activity and antidiabetic potential (FEI, FEL, FIE, FKN, FGKG, and MEE). FEI, FEL, and FIE were in the same chromatographic peak and this mixture showed the best ABTS scavenging (78.25%) and DPP4 inhibition (IC50 = 4.20 µg/ml). MEE showed the best DPPH scavenging (47%). FGKG showed the best inhibition of α‐amylase (54%) and α‐glucosidase (56%) and may be a competitive inhibitor based on in silico‐predicted interactions with catalytic amino acids in the active site of both enzymes. These peptides could be used as nutraceutical supplements against diseases related to oxidative stress and diabetes. Practical Application This study showed that chickpea protein hydrolyzates are good sources of peptides with antidiabetic potential, showing high antioxidant activity and inhibition of enzymes related to carbohydrate metabolism and type 2 diabetes. These hydrolyzates could be formulated in functional foods for diabetes.

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Section: Resultssupporting

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates

Quintero‐Soto

Chávez-Ontiveros

Garzón‐Tiznado

et al. 2021

Journal of Food Science

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“…The chickpea has also been found to have beneficial effects in the prevention of diabetes, cardiovascular disease and cancer [ 2 ]. Additionally, chickpea protein isolated from chickpea flour and further digested by a variety of peptidases or acid–base methods has shown several bioactivities [ 3 , 4 ]. However, food products based on chickpea protein hydrolysates are not widely marketed.…”

Section: Introductionmentioning

confidence: 99%

“…Previously published studies have largely focused on the enzymes present in the human digestive system, as well as alcalase and flavourzyme [ 4 ]. To the best of our knowledge, there are limited results for the sequences of peptides obtained from chickpeas produced using bromelain.…”

Section: Introductionmentioning

confidence: 99%

Identification and Comparison of Peptides from Chickpea Protein Hydrolysates Using Either Bromelain or Gastrointestinal Enzymes and Their Relationship with Markers of Type 2 Diabetes and Bitterness

2020

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The chickpea (Cicer arietinum L.) is one of the most important pulses worldwide. The objective was to identify, compare and evaluate peptides from chickpea hydrolysates produced by two enzymatic treatments. The antidiabetic potential and bitterness of the peptides and induction of bitter receptors were identified in silico. Proteins were isolated from the Kabuli variety. Peptides were produced from the proteins using a simulated digestive system (pepsin/pancreatin, 1:50 Enzyme/Protein, E/P), and these peptides were compared with those produced via bromelain hydrolysis (1:50 E/P). The protein profiles, sequences and characteristics of the peptides were evaluated. The biochemical inhibition and molecular docking of dipeptidyl peptidase-IV (DPP-IV), α-amylase and α-glucosidase were also studied. The molecular docking identified peptides from enzymatic hydrolysis as inhibitors of DPP-IV. The high hydrophobicity of the peptides indicated the potential for bitterness. There was no correlation between peptide length and DPP-IV binding. Peptides sequenced from the pepsin/pancreatin hydrolysates, PHPATSGGGL and YVDGSGTPLT, had greater affinity for the DPP-IV catalytic site than the peptides from the bromelain hydrolysates. These results are in agreement with their biochemical inhibition, when considering the inhibition of sitagliptin (54.3 µg/mL) as a standard. The bitter receptors hTAS2R38, hTAS2R5, hTAS2R7 and hTAS2R14 were stimulated by most sequences, which could be beneficial in the treatment of type 2 diabetes. Chickpea hydrolysates could be utilized as functional ingredients to be included in the diet for the prevention of diabetes.

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“…Combined with the enzyme biduri can increase the degree of hydrolysis because the enzyme bidur as exopeptidase cuts peptide bonds resulting from cutting papain at the end. This is following the study of Xu et al, (2019) that endopeptidases hydrolyzes proteins and increases the amount of N-terminal for further hydrolysis by exopeptidase.…”

Section: Degree Of Hydrolysismentioning

confidence: 99%

Physicochemical and Organoleptic Characteristics of Seasoning from Tempe Hydrolysates using Long Treatment of Fermentation and Proteolytic Enzyme Proportion

Putri

Winarti

Djajati

2020

Nusantara Science and Technology Proceedings

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Tempeh is a native Nusantara food that is often found in traditional Indonesian markets. Over fermentation, due to unsold, they are called over fermented tempeh resulted in non-optimum utilization. Alternative utilizations that can be used is as a seasoning. The making of seasoning can be done by the hydrolysis technique using the protease enzyme of biduri and papain. This study aimed to determine the effect of fermentation time and the proportion of proteolytic enzyme on the physicochemical and organoleptic properties of seasoning from tempeh hydrolysates. The experimental design used was a factorial pattern CRD with two factors. Factor I is tempeh fermentation time (18 hours and 72 hours), while factor II is the enzyme proportion of biduri and papain (0%: 100%; 25%: 75%; 50%: 50%; 75%: 25%; and 100 %: 0%). The best treatment is 72 hours fermentation duration and the enzyme proportion of biduri and papain (50%: 50%) which produces a seasoning powder with the following characteristics: the degree of hydrolysis 82.32%; dissolved protein 58.85%; moisture 7.89%; water solubility index 0.09 gr/ml; oil absorption 0.78 ml/gr, yield 9.32%, organoleptic to taste 3.93 (savory), aroma 3.40 (somewhat pleasant), and color 1.13 (very not white), and glutamic acid content 59, 93 mg/100 gr.

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Effect of enzymatic hydrolysis using endo- and exo-proteases on secondary structure, functional, and antioxidant properties of chickpea protein hydrolysates

Cited by 66 publications

References 39 publications

Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates

Characterization of peptides with antioxidant activity and antidiabetic potential obtained from chickpea (Cicer arietinum L.) protein hydrolyzates

Identification and Comparison of Peptides from Chickpea Protein Hydrolysates Using Either Bromelain or Gastrointestinal Enzymes and Their Relationship with Markers of Type 2 Diabetes and Bitterness

Physicochemical and Organoleptic Characteristics of Seasoning from Tempe Hydrolysates using Long Treatment of Fermentation and Proteolytic Enzyme Proportion

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