scholarly journals Identification of zinc-binding peptides in ADAM17-inhibiting whey protein hydrolysates using IMAC-Zn2+ coupled with shotgun peptidomics

2021 ◽  
Vol 3 (1) ◽  
Author(s):  
M. Chinonye Udechukwu ◽  
Chi Dang ◽  
Chibuike C. Udenigwe
Keyword(s):  
Whey Protein ◽  
Binding Capacity ◽  
Folate Receptor ◽  
Protein Hydrolysates ◽  
Zinc Binding ◽  
Whey Protein Hydrolysates ◽  
Peptide Fraction ◽  
Binding Peptides ◽  
A Disintegrin And Metalloproteinase ◽  
Chain Lengths

Abstract Food components possessing zinc ligands can be used to inhibit zinc-dependent enzymes. In this study, zinc-binding peptides were derived from whey protein hydrolysates, and their ultrafiltration (> 1 and < 1 kDa) fractions, produced with Esperase (WPH-Esp), Everlase and Savinase. Immobilized metal affinity chromatography (IMAC-Zn2+) increased the zinc-binding capacity of the peptide fraction (83%) when compared to WPH-Esp (23%) and its < 1 kDa fraction (40%). The increased zinc-binding capacity of the sample increased the inhibitory activity against the zinc-dependent “a disintegrin and metalloproteinase 17”. LC-MS/MS analysis using a shotgun peptidomics approach resulted in the identification of 24 peptides originating from bovine β-lactoglobulin, α-lactalbumin, serum albumin, β-casein, κ-casein, osteopontin-k, and folate receptor-α in the fraction. The identified peptides contained different combinations of the strong zinc-binding group of residues, His+Cys, Asp+Glu and Phe+Tyr, although Cys residues were absent in the sequences. In silico predictions showed that the IMAC-Zn2+ peptides were non-toxins. However, the peptides possessed poor drug-like and pharmacokinetic properties; this was possibly due to their long chain lengths (5–19 residues). Taken together, this work provided an array of food peptide-based zinc ligands for further investigation of structure-function relationships and development of nutraceuticals against inflammatory and other zinc-related diseases. Graphical abstract

Iron-binding peptides from whey protein hydrolysates: Evaluation, isolation and sequencing by LC–MS/MS

2015 ◽  
Vol 71 ◽  
pp. 132-139 ◽  
Author(s):  
Maria Elisa Caetano-Silva ◽  
Maria Teresa Bertoldo-Pacheco ◽  
Adriana Franco Paes-Leme ◽  
Flavia Maria Netto
Keyword(s):  
Whey Protein ◽  
Protein Hydrolysates ◽  
Iron Binding ◽  
Whey Protein Hydrolysates ◽  
Binding Peptides

Investigation of potent odorants generated during the production of whey protein hydrolysates

2018 ◽  
Vol 89 (9) ◽  
pp. 1348-1354 ◽  
Author(s):  
Hajime Nakada ◽  
Motoko Ohata ◽  
Mari Hosaka ◽  
Hiroshi Ochi ◽  
Fumiaki Abe ◽  
...  
Keyword(s):  
Whey Protein ◽  
Protein Hydrolysates ◽  
Whey Protein Hydrolysates ◽  
Potent Odorants

Encapsulation of Bacillus subtilis Cells for Production of Whey Protein Hydrolysates

2018 ◽  
Vol 54 (6) ◽  
pp. 624-630
Author(s):  
Y. Alvarado ◽  
C. Muro ◽  
I. A. Rivero ◽  
G. E. Pina ◽  
J. Illescas ◽  
...  
Keyword(s):  
Bacillus Subtilis ◽  
Whey Protein ◽  
Protein Hydrolysates ◽  
Whey Protein Hydrolysates

scholarly journals Peptide Analysis and the Bioactivity of Whey Protein Hydrolysates from Cheese Whey with Several Enzymes

2017 ◽  
Vol 37 (1) ◽  
pp. 62-70 ◽  
Author(s):  
Renda Kankanamge Chaturika Jeewanthi ◽  
Myeong Hee Kim ◽  
Na-Kyoung Lee ◽  
Yoh Chang Yoon ◽  
Hyun-Dong Paik
Keyword(s):  
Whey Protein ◽  
Cheese Whey ◽  
Protein Hydrolysates ◽  
Peptide Analysis ◽  
Whey Protein Hydrolysates

scholarly journals In Vitro Characterisation of the Antioxidative Properties of Whey Protein Hydrolysates Generated under pH- and Non pH-Controlled Conditions

Foods ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 582 ◽  
Author(s):  
Thanyaporn Kleekayai ◽  
Aurélien V. Le Gouic ◽  
Barbara Deracinois ◽  
Benoit Cudennec ◽  
Richard J. FitzGerald
Keyword(s):  
Whey Protein ◽  
Protein Hydrolysates ◽  
Whey Protein Concentrate ◽  
Trolox Equivalent Antioxidant Capacity ◽  
Ros Generation ◽  
Whey Protein Hydrolysates ◽  
Hydrolysis Conditions ◽  
The Impact ◽  
Ph Controlled

Bovine whey protein concentrate (WPC) was hydrolysed under pH-stat (ST) and non pH-controlled (free-fall, FF) conditions using Debitrase (DBT) and FlavorPro Whey (FPW). The resultant whey protein hydrolysates (WPHs) were assessed for the impact of hydrolysis conditions on the physicochemical and the in vitro antioxidant and intracellular reactive oxygen species (ROS) generation in oxidatively stressed HepG2 cells. Enzyme and hydrolysis condition dependent differences in the physicochemical properties of the hydrolysates were observed, however, the extent of hydrolysis was similar under ST and FF conditions. Significantly higher (p < 0.05) in vitro and cellular antioxidant activities were observed for the DBT compared to the FPW–WPHs. The WPHs generated under ST conditions displayed significantly higher (p < 0.05) oxygen radical absorbance capacity (ORAC) and Trolox equivalent antioxidant capacity (TEAC) values compared to the FF-WPHs. The impact of hydrolysis conditions was more pronounced in the in vitro compared to the cellular antioxidant assay. WPH peptide profiles (LC-MS/MS) were also enzyme and hydrolysis conditions dependent as illustrated in the case of β-lactoglobulin. Therefore, variation in the profiles of the peptides released may explain the observed differences in the antioxidant activity. Targeted generation of antioxidant hydrolysates needs to consider the hydrolysis conditions and the antioxidant assessment method employed.

scholarly journals Soluble Whey Protein Hydrolysate Ameliorates Muscle Atrophy Induced by Immobilization via Regulating the PI3K/Akt Pathway in C57BL/6 Mice

Nutrients ◽  
2020 ◽  
Vol 12 (11) ◽  
pp. 3362
Author(s):  
Ji Eun Shin ◽  
Seok Jun Park ◽  
Seung Il Ahn ◽  
Se-Young Choung
Keyword(s):  
Skeletal Muscle ◽  
Whey Protein ◽  
Muscle Mass ◽  
Muscle Atrophy ◽  
Skeletal Muscle Mass ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Protein Supplementation ◽  
Whey Protein Hydrolysates ◽  
Whey Protein Hydrolysate

Sarcopenia, a loss of skeletal muscle mass and function, is prevalent in older people and associated with functional decline and mortality. Protein supplementation is necessary to maintain skeletal muscle mass and whey protein hydrolysates have the best nutrient quality among food proteins. In the first study, C57BL/6 mice were subjected to immobilization for 1 week to induce muscle atrophy. Then, mice were administered with four different whey protein hydrolysates for 2 weeks with continuous immobilization. Among them, soluble whey protein hydrolysate (WP-S) had the greatest increase in grip strength, muscle weight, and cross-sectional area of muscle fiber than other whey protein hydrolysates. To investigate the molecular mechanism, we conducted another experiment with the same experimental design. WP-S significantly promoted the phosphoinositide 3-kinase (PI3K)/protein kinase B (Akt)/mammalian target of rapamycin (mTOR) pathway and inhibited the PI3K/Akt/forkhead box O (FoxO) pathway. In addition, it increased myosin heavy chain (MyHC) expression in both the soleus and quadriceps and changed MyHC isoform expressions. In conclusion, WP-S attenuated muscle atrophy induced by immobilization by enhancing the net protein content regulating muscle protein synthesis and degradation. Thus, it is a necessary and probable candidate for developing functional food to prevent sarcopenia.

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