Towards the design of hypolipidaemic peptides: Deoxycholate binding affinity of hydrophobic peptide aggregates of casein plastein

Mohan, Aishwarya; Udenigwe, Chibuike C.

doi:10.1016/j.jff.2015.06.064

Cited by 29 publications

(15 citation statements)

References 23 publications

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“…Surface hydrophobicity of the hydrolysates was analyzed using previously reported methods (Alizadeh‐Pasdar & Li‐Chan, ; Mohan & Udenigwe, ). 8‐Anilo‐1‐naphthalenesulfonic acid (1 µl of 0.008 M) was added to 200 µl of five concentrations of the protein hydrolysates (0.125, 0.25, 0.5, 1, and 2 mg/ml) in a Grenier UV‐Star 96‐well black microplate.…”

Section: Methodsmentioning

confidence: 99%

“…Pico‐Tag method of precolumn derivatization was performed with phenyl isothiocyanate at room temperature. Resulting amino acid derivatives were dissolved in phosphate buffer and ultra‐performance liquid chromatography (10‐cm C‐18 column; 0.21 × 10 cm) was performed using a Waters ACQUITY UPLC (Milford, MA, USA), as previously reported (Mohan & Udenigwe, ). UV detection of peaks was conducted at 254 nm and results expressed as percent amino acid composition.…”

Section: Methodsmentioning

confidence: 99%

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Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Boachie

Okoro²,

Imai

et al. 2019

J Food Biochem

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Abbreviations: ANS, 8-anilino-1-naphthalenesulphonic acid; BSA, bovine serum albumin; DPP-4, dipeptidyl peptidase-4; GIP, glucose-dependent insulinotropic polypeptide; GLP-1, glucagon-like peptide-1; GRAVY, grand average of hydropathicity; OPA, o-phthalaldehyde; pI, theoretical isoelectric point; RMSE, root mean square error; T2DM, type 2 diabetes mellitus; UPLC, ultra-performance liquid chromatography. AbstractIn silico and in vitro parameters were used to assess the potential of pigeon pea (Cajanus cajan) nutrient reservoir proteins as sources of dipeptidyl peptidase (DPP)-4 inhibitors. In silico, 40 pigeon pea proteins evaluated had 46% of amino acids associated with DPP-4 inhibition. After virtual hydrolysis, pepsin had the highest frequency of release and bioactivity of released DPP-4 inhibiting peptides, compared to papain and thermolysin. In vitro, thermolysin released the most active DPP-4 inhibitors.The protein hydrolysates contained similar amino acids but different particle sizes.Thus, the bioactivity patterns are attributable to the different nature and behavior of proteins/peptides under actual and virtual conditions. Using eight physicochemical variables, a random forest model with moderate prediction accuracy was developed for predicting DPP-4 inhibitory activity of papain hydrolysates. The findings demonstrate that proteins from pigeon pea are precursors of DPP-4 inhibitors, with potential use in formulating functional food for managing type 2 diabetes. | In silico analysis of physicochemical properties of pigeon pea proteinsPhysicochemical properties of the 40 mature pigeon pea proteins/ domains and BSA were calculated using the ProtParam feature of UniProtKB. The properties include the protein chain length, theoretical isoelectric point (pI), molecular weight, grand average of K E Y W O R D S bioactive peptides, bioinformatics, Cajanus cajan, dipeptidyl peptidase-4, in silico, pigeon pea S U PP O RTI N G I N FO R M ATI O N Additional supporting information may be found online in the Supporting Information section at the end of the article. How to cite this article: Boachie RT, Okoro FL, Imai K, et al. Enzymatic release of dipeptidyl peptidase-4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments. J Food Biochem.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Boachie

Okoro²,

Imai

et al. 2019

J Food Biochem

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“…Amino acid composition (%) of NC and CP was analyzed at the SPARC BioCentre, The Hospital for Sick Children (Toronto, Canada), using the Pico-Tag method after vapor-phase hydrolysis with 6 M HCl/1% phenol at 110°C for 24 hr, pre-column derivatization with phenyl isothiocyanate, and reverse-phase ultra-performance liquid chromatography using a Waters ACQUITY UPLC (Milford, MA, USA), as previously reported (Mohan & Udenigwe, 2015).…”

Section: Amino Acid Composition Of the Proteinsmentioning

confidence: 99%

“…Surface hydrophobicity of NC and CP was determined using the fluorescent probe, 8-anilino-1-naphthalenesulphonic acid (ANS), as described by Mohan and Udenigwe (2015). Surface hydrophobicity was obtained as the slope of the fluorescence intensity versus concentration plot.…”

Section: Protein Surface Hydrophobicitymentioning

confidence: 99%

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase‐IV inhibitors

et al. 2019

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Bioinformatics was applied for strategic processing of yellow mealworm (Tenebrio molitor) proteins to produce dipeptidyl peptidase (DPP)-IV inhibiting peptides. In silico analysis of 384 mealworm proteins revealed structural proteins as better precursors of DPP-IV inhibiting peptides, compared with other protein types, after pepsin and papain hydrolysis. This was associated with the higher hydropathicity and amounts of residues associated with DPP-IV inhibition in the structural (cuticular) proteins. In silico, the peptides were mostly released with pepsin than papain. Cuticular (CP) and non-cuticular proteins (NC) were extracted from yellow mealworm and hydrolyzed with pepsin and papain in vitro to validate the virtual findings. CP hydrolysate with papain inhibited DPP-IV the most compared to CP hydrolysate with pepsin, whereas NC hydrolysates were mostly inactive. CP had higher hydrophobic-hydrophilic amino acid ratios and contents of the activity-associated residues than NC. The findings demonstrate the application of bioinformatics in processing proteins for bioactive peptide production. S U PP O RTI N G I N FO R M ATI O NAdditional supporting information may be found online in the Supporting Information section.How to cite this article: Dávalos Terán I, Imai K, Lacroix IME, Fogliano V, Udenigwe CC. Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase-IV inhibitors. J Food Biochem. 2020;44:e13121. https ://doi.

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“…8‐Anilino‐1‐naphthalenesulphonic acid (ANS, Sigma‐Aldrich, ON, Canada), a hydrophobic probe, was used in the determination of S o (Mohan & Udenigwe, ). Sample (0.0300–0.0009%, 100 µL) was mixed with 100 µL of ANS (0.04 mM) in a 96‐well fluorescence plate.…”

Section: Methodsmentioning

confidence: 99%

Yield, physicochemical, and antioxidant properties of Atlantic salmon visceral hydrolysate: Comparison of lactic acid bacterial fermentation with Flavourzyme proteolysis and formic acid treatment

Rajendran

Mohan

Khiari

et al. 2018

J Food Process Preserv

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This study compares a cost‐effective microbial method, involving lactic acid (LA) fermentation, with the conventional formic acid (FA) treatment and Flavourzyme (FL) enzymatic hydrolysis for valorizing Atlantic salmon processing waste (Viscera). LA and FA processing approaches relied on production (LA) or addition (FA) of organic acids to lower the pH and activate the inherent proteases in these tissues, whereas FL processing was carried out at the optimum conditions for Flavourzyme (37 °C, pH 7.0). Highest protein hydrolysate fraction recovery (∼57%) was seen in LA fermentation, while FA processing resulted in the highest protein levels (∼87%) in the recovered hydrolysate fraction and lowest residual fraction (∼4%). In general, FL processing demonstrated higher Fe(II) chelation (73%) and ferric reducing capacity (27 mM glutathione equivalent) whereas LA‐hydrolysates showed enhanced sacrificial antioxidant properties. Findings from this study would have implications on the application and production of salmon‐based protein hydrolysates, especially, from the perspective of their functionality. Practical applications Peptides derived from natural sources such as fish products have been extensively reported to exert antioxidant activity that mitigates oxidative stress and providing beneficial effects to human health as well as food storage. Several sources of proteins are being explored for the production of biologically active peptides. Utilizing by‐product streams such as fish processing waste is especially attractive as these are cheaper and rich sources of protein. Therefore, utilizing marine bioprocessing waste for the production food‐grade protein hydrolysates is promising, especially in Atlantic Canada.

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Towards the design of hypolipidaemic peptides: Deoxycholate binding affinity of hydrophobic peptide aggregates of casein plastein

Cited by 29 publications

References 23 publications

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Enzymatic release of dipeptidyl peptidase‐4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments

Bioinformatics of edible yellow mealworm (Tenebrio molitor) proteome reveal the cuticular proteins as promising precursors of dipeptidyl peptidase‐IV inhibitors

Yield, physicochemical, and antioxidant properties of Atlantic salmon visceral hydrolysate: Comparison of lactic acid bacterial fermentation with Flavourzyme proteolysis and formic acid treatment

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