Antibacterial effect and hydrophobicity of yak κ-casein hydrolysate and its fractions

Cheng, Xue; Tang, Xi; Wang, Q.; Mao, Xiaoman

doi:10.1016/j.idairyj.2012.12.004

Cited by 27 publications

(6 citation statements)

References 40 publications

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“…After that, the hydrolysis rate decreased, which might be a result of the reduction in available cleavage sites for the enzymes. The typical shape of hydrolysis curves was found previously for cow’s milk protein hydrolysates ( 30 ) and goat’s milk protein hydrolysates ( 31 ).…”

Section: Resultssupporting

confidence: 76%

Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Oussaief

Jrad

Adt

et al. 2020

Food technol. biotechnol. (Online)

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Research background. Milk protein hydrolysates have received particular attention due to their health-promoting effects. Dromedary milk differs from the milk of other dairy animals in the composition and structure of its protein components, which give it unique properties. The bioactivity and functionality of whole dromedary milk proteins and their enzymatic hydrolysates have not received much attention, hence this study aims to investigate the effect of enzymatic hydrolysis of dromedary milk proteins on their antioxidant activities and functional properties. Experimental approach. Dromedary milk proteins were treated using four proteolytic enzymes (pepsin, trypsin, α-chymotrypsin and papain) and two mixtures of enzymes (pancreatin and pronase). The degree of hydrolysis was measured to verify the hydrolysis of the proteins. The sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and gel filtration chromatography served to determine the molecular mass distribution of the hydrolysates while reversed phase-high performance liquid chromatography (RP-HPLC) was conducted to explore their hydrophobicity. The antioxidant activities were evaluated using various in vitro tests, including 2,2-diphenyl-1-picrylhydrazyl (DPPH) and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid (ABTS) radical scavenging capacities, iron(III) reducing ability and chelating activity. Besides, functional properties such as solubility, foaming and emulsification were assessed. Results and conclusions. Dromedary milk protein hydrolysates exhibited different degrees of hydrolysis ranging from 17.69 to 41.86 %. Apart from that, the hydrolysates showed different electrophoretic patterns, molecular mass distribution and RP-HPLC profiles demonstrating the heterogeneity of the resulting peptides in terms of molecular mass and polarity. The hydrolysates displayed significantly higher antioxidant capacities than the undigested proteins at all the tested concentrations. Iron(II) chelating activity was the most improved assay after proteolysis and the hydrolysate generated with pancreatin had the highest chelating power. Dromedary milk protein hydrolysates possessed good solubility (>89 %). Further, foaming and emulsifying properties of dromedary milk proteins were enhanced after their proteolysis. These interfacial properties were influenced by the enzymes employed during proteolysis. Novelty and scientific contribution. Enzymatic hydrolysis of dromedary milk proteins is an effective tool to obtain protein hydrolysates with great antioxidant and functional properties. These results suggest that dromedary milk protein hydrolysates could be used as a natural source of antioxidant peptides to formulate functional foods and nutraceuticals.

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Section: Resultssupporting

confidence: 76%

Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Oussaief

Jrad

Adt

et al. 2020

Food technol. biotechnol. (Online)

View full text Add to dashboard Cite

show abstract

“…In our study, the DH had no significant effect (p > 0.05) on antibacterial activity. [15] and [44] observed similar results in their studies on trout protein hydrolysate and yak kappa-casein hydrolysate, respectively. The biological attributes of peptides are largely influenced by their molecular structural properties, including amino acid composition, sequence, net charge, and chain length [43].…”

Section: Discussionsupporting

confidence: 63%

“…These properties may have influenced the antibacterial activities of the collagen hydrolysates. Notably, hydrophobicity is thought to be important because it facilitates the interaction of the peptides with bacterial cytoplasmic membranes [ 44 ]. This feature relates more to the molecular hydrophobicity of individual peptides instead of surface hydrophobicity.…”

Section: Discussionmentioning

confidence: 99%

Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes

et al. 2021

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This study investigated peptide fractions from fish skin collagen for antibacterial activity against Escherichia coli and Salmonella strains. The collagen was hydrolyzed with six commercial proteases, including trypsin, Alcalase, Neutrase, Flavourzyme, pepsin and papain. Hydrolyzed samples obtained with trypsin and Alcalase had the largest number of small peptides (molecular weight < 10 kDa), while the hydrolysate produced with papain showed the lowest degree of hydrolysis and highest number of large peptides. Four hydrolysates were found to inhibit the growth of the Gram-negative bacteria, with papain hydrolysate showing the best activity against E. coli, and Neutrase and papain hydrolysates showing the best activity against S. abony; hydrolysates produced with trypsin and pepsin did not show detectable antibacterial activity. After acetone fractionation of the latter hydrolysates, the peptide fractions demonstrated enhanced dose-dependent inhibition of the growth (colony-forming units) of four Salmonella strains, including S. abony (NCTC 6017), S. typhimurium (ATCC 13311), S. typhimurium (ATCC 14028) and S. chol (ATCC 10708). Shotgun peptidomics analysis of the acetone fractions of Neutrase and papain hydrolysates resulted in the identification of 71 and 103 peptides, respectively, with chain lengths of 6–22 and 6–24, respectively. This work provided an array of peptide sequences from fish skin collagen for pharmacophore identification, structure–activity relationship studies, and further investigation as food-based antibacterial agents against pathogenic microorganisms.

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“…As the use of microbial proteases is simple, non-expensive, and completely safe, it is the preferred methodology for hydrolysis processes compared with the other commercial proteases from plant and animal origin [4]. The resulting hydrolyzed proteins and peptides have been described to exert an important biological role, including antioxidant [5], antimicrobial [6], anticancer [5], antidiabetic [7], and antihypertensive activities [8]. They also influence the cardiovascular, immune, nervous, and gastrointestinal systems [8,9].…”

Section: Introductionmentioning

confidence: 99%

Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products

Mazloomi

Mora

Aristoy

et al. 2020

Foods

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In this study, orange seed proteins were hydrolyzed by Alcalase enzyme at different enzyme concentrations 1–3% (v/w) and hydrolysis times (2–5 h), to obtain bioactive peptides showing antioxidant, Angiotensin-converting enzyme (ACE) -inhibitory, and hypoglycemic activities. The highest biological activities (p < 0.05) were achieved by using a hydrolysis time of 5 h and an enzyme concentration of 2%. Orange seed protein hydrolysate (OSPH) was prepared under these conditions, and peptides were isolated and purified by using size-exclusion chromatography and high-performance liquid chromatography, respectively. The fractions that showed the highest biological activities were analyzed by mass spectrometry in tandem, and a total of 63 peptide sequences were found. Moreover, the effect of simulated gastrointestinal digestion on the bioactivity of the fractions was studied, and the novel peptide sequences generated were also identified. Overall, despite there being some differences in the profile of peptide sequences obtained, the main results showed non-significant differences in the analyzed bioactivities after simulated gastrointestinal digestion.

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Antibacterial effect and hydrophobicity of yak κ-casein hydrolysate and its fractions

Cited by 27 publications

References 40 publications

Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Dromedary Milk Protein Hydrolysates Show Enhanced Antioxidant and Functional Properties

Anti-Salmonella Activity and Peptidomic Profiling of Peptide Fractions Produced from Sturgeon Fish Skin Collagen (Huso huso) Using Commercial Enzymes

Impact of Simulated Gastrointestinal Digestion on the Biological Activity of an Alcalase Hydrolysate of Orange Seed (Siavaraze, Citrus sinensis) by-Products

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