Antioxidant, tyrosinase and urease inhibitory activities of camel αS-casein and its hydrolysate fractions

Addar, Lydia; Bensouici, Chawki; Zennia, Saliha Si Ahmed; Haroun, Saliha Boudjenah; Mati, Abderrahmane

doi:10.1016/j.smallrumres.2019.01.015

Cited by 25 publications

(11 citation statements)

References 37 publications

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“…This could be correlated to the biological action of the amino acids incorporated into this low molecular weight fraction. These results are in line with the results of Salami et al [ 25 ] and Addar et al [ 29 ], who reported that the low molecular weight fractions of camel αS-casein hydrolyzed with trypsin displayed higher antioxidant activity than the high molecular weight fractions and the total hydrolysate]. Likewise, Salami et al stated that the retentate of 5 kDa fraction of the whole camel casein hydrolyzed by pepsin, chymotrypsin, or trypsin showed higher antioxidant activity compared to the total hydrolysates [ 25 ].…”

Section: Resultssupporting

confidence: 93%

“…The antioxidant activity of the papain hydrolyzed CWPH was several times higher ( p ˂ 0.05) than that of the unhydrolyzed CWP. Similarly, the hydrolysis of camel whey proteins, camel whole casein, camel β-casein, and camel αS-casein by pepsin, proteinase K, thermolysin, trypsin, or chymotrypsin increased significantly their antioxidant activities [ 29 , 30 ]. In addition, papain and Alcalase hydrolysates of camel casein displayed antioxidant activity [ 31 ].…”

Section: Resultsmentioning

confidence: 99%

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Angiotensin-I Converting Enzyme Inhibition and Antioxidant Activity of Papain-Hydrolyzed Camel Whey Protein and Its Hepato-Renal Protective Effects in Thioacetamide-Induced Toxicity

Osman

El-Hadary

Korish

et al. 2021

Foods

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Papain hydrolysis of camel whey protein (CWP) produced CWP hydrolysate (CWPH). Fractionation of CWPH by the size exclusion chromatography (SEC) generated fractions (i.e., SEC-F1 and SEC-F2). The angiotensin- converting- enzyme inhibitory activity (ACE-IA) and free radical scavenging actions were assessed for CWP, CWPH, SEC-F1, and SEC-F2. The SEC-F2 exerted the highest ACE-IA and scavenging activities, followed by CWPH. The protective effects of CWPH on thioacetamide (TAA)-induced toxicity were investigated in rats. The liver enzymes, protein profile, lipid profile, antioxidant enzyme activities, renal functions, and liver histopathological changes were assessed. Animals with TAA toxicity showed impaired hepatorenal functions, hyperlipidemia, and decreased antioxidant capacity. Treatment by CWPH counteracted the TAA-induced oxidative tissue damage as well as preserved the renal and liver functions, the antioxidative enzyme activities, and the lipid profile, compared to the untreated animals. The current findings demonstrate that the ACE-IA and antioxidative effects of CWPH and its SEC-F2 fraction are worth noting. In addition, the CWPH antioxidative properties counteracted the toxic hepatorenal dysfunctions. It is concluded that the hydrolysis of CWP generates a wide range of bioactive peptides with potent antihypertensive, antioxidant, and hepatorenal protective properties. This opens up new prospects for the therapeutic utilization of CWPH and its fractions in the treatment of oxidative stress-associated health problems, e.g., hypertension and hepatorenal failure.

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Section: Resultssupporting

confidence: 93%

Section: Resultsmentioning

confidence: 99%

Angiotensin-I Converting Enzyme Inhibition and Antioxidant Activity of Papain-Hydrolyzed Camel Whey Protein and Its Hepato-Renal Protective Effects in Thioacetamide-Induced Toxicity

Osman

El-Hadary

Korish

et al. 2021

Foods

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“…Also, the obtained fractions were considered from molecular weight point of view in each hydrolysate, lower and higher than 10 kDa. The results showed that low molecular weight fractions (<10 kDa) had better inhibitory effects than those of high molecular weight (>10 kDa) and un‐hydrolyzed fractions at the same concentrations 52 …”

Section: Natural Peptidesmentioning

confidence: 99%

“…The results showed that low molecular weight fractions (<10 kDa) had better inhibitory effects than those of high molecular weight (>10 kDa) and un-hydrolyzed fractions at the same concentrations. 52 Huang et al have recently studied Chinese quince seed proteins for its tyrosinase inhibitory activity. Enzymatic hydrolyzation of proteins gave two main sequences: NYRRE (asparagine-tyrosinearginine-arginine-glutamic acid) and RHAKF (arginine-histidinealanine-lysine-phenylalanine), which showed anti-tyrosine effects.…”

Section: Kawagishia Et Al Drew Out Anti-tyrosinase Cyclotetrapeptide Frommentioning

confidence: 99%

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Hariri

Saeedi

Akbarzadeh

2021

Journal of Peptide Science

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Tyrosinase is a copper‐containing enzyme involved in the biosynthesis of melanin pigment, which is the most important photo protective agent against skin photo carcinogenesis. Excess production of melanin causes hyperpigmentation leading to undesired browning in human skin, fruits, and vegetable as well as plant‐derived foods. Moreover, the role of tyrosinase in the onset and progression of various diseases such as cancers, Alzheimer's, and Parkinson diseases has been well documented in the literature. In this respect, tyrosinase inhibitors have been in the center of attention particularly as the efficient skin whitening agents. Among a wide range of compounds possessing anti‐tyrosinase activity, peptides both natural and synthetic derivatives have attracted attention due to high potency and safety.

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“…Herein, we aim at defining bioactive tetrapeptide sequences that are derived from milk protein hydrolysates and efficiently downregulate melanin synthesis. We explored the tyrosinase inhibitory activities of peptides that were derived from κ-casein and β-lactoglobulin and were isolated and identified as antioxidants [ 31 , 32 ] since several studies have shown that the antioxidant properties of peptides and their tyrosinase inhibitory activity are related [ 17 , 33 ]. Kim’s group previously reported the dual antioxidant and tyrosinase inhibitory activities of caffeic acid-β-lactoglobulin peptide derivatives [ 34 ] but these activities were mainly due to the caffeic acid moiety.…”

Section: Introductionmentioning

confidence: 99%

Milk Protein-Derived Antioxidant Tetrapeptides as Potential Hypopigmenting Agents

et al. 2020

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Excessive accumulation of melanin can cause skin pigmentation disorders, which may be accompanied by significant psychological stress. Although many natural and synthetic products have been developed for the regulation of melanogenesis biochemistry, the management of unwanted skin pigmentation remains challenging. Herein, we investigated the potential hypopigmenting properties of peptide sequences that originated from milk proteins such as ĸ-casein and β-lactoglobulin. These proteins are known to inhibit melanogenesis and their hydrolysates are reported as antioxidant peptides. We synthesize tetrapeptide fragments of the milk protein hydrolysates and investigate the amino acids that are essential for designing peptides with tyrosinase inhibitory and antioxidant activities. We found that the peptide methionine-histidine-isoleucine-arginine amide sufficiently inhibits mushroom tyrosinase activity, shows potent antioxidant activity and effectively impedes melanogenesis in cultured melanocytes via cooperative biological activities. Our findings demonstrate the potential utility of the bioactive tetrapeptide from milk proteins as a chemical alternative to hypopigmenting agents.

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Antioxidant, tyrosinase and urease inhibitory activities of camel αS-casein and its hydrolysate fractions

Cited by 25 publications

References 37 publications

Angiotensin-I Converting Enzyme Inhibition and Antioxidant Activity of Papain-Hydrolyzed Camel Whey Protein and Its Hepato-Renal Protective Effects in Thioacetamide-Induced Toxicity

Angiotensin-I Converting Enzyme Inhibition and Antioxidant Activity of Papain-Hydrolyzed Camel Whey Protein and Its Hepato-Renal Protective Effects in Thioacetamide-Induced Toxicity

Naturally occurring and synthetic peptides: Efficient tyrosinase inhibitors

Milk Protein-Derived Antioxidant Tetrapeptides as Potential Hypopigmenting Agents

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