Enzymatic digestion and antioxidant activity of the native and molten globule states of camel α-lactalbumin: Possible significance for use in infant formula

Salami, Maryam; Yousefi, Reza; Ehsani, Mohammad Reza; Razavi, Seyed Hadi; Chobert, Jean‐Marc; Haertlé, Thomas; Saboury, Ali Akbar; Atri, Maliheh Sadat; Niasari-Naslaji, Amir; Ahmad, Faizan; Moosavi-Movahedi, Ali Akbar

doi:10.1016/j.idairyj.2009.02.007

Cited by 86 publications

(43 citation statements)

References 34 publications

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“…This value was, however, lower than that found by Salami et al (2009) for the camel α-LA (3 µmol L -1 ). This difference could be explained by the fact that F1 was a mixture of several proteins that underestimated the TEAC value of α-LA contained in F1.…”

Section: Investigation Of Radical-scavenging Activitycontrasting

confidence: 72%

“…The camel α-LA possesses five Trp residues on its sequence, whereas the bovine counterpart contains only four. The presence of an additional Trp residue in the case of the camel sequence might contribute to its better radical scavenging power than that of the bovine protein reported by Salami et al (2009).…”

Section: Investigation Of Radical-scavenging Activitymentioning

confidence: 80%

“…An advantage of α-LA may be its beneficial role in the antioxidant system of the neonate (Lien, 2003). The bovine α-LA (Sadat et al, 2011) and the camel α-LA (Salami et al, 2009; are a source of free radical-scavenging peptides. Therefore, attention is being focused on producing α-LA-enriched formulae because α-LA might have an ability to attenuate oxidative stress occurring in inflammatory bowel disease after oral administration (IBD; Rezaie et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Fast protein liquid chromatography of camel ?-lactalbumin fraction with radical scavenging activity

Halima

Jrad

Khorchani

et al. 2014

Emir. J. Food Agric

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The aim of this study was to investigate the radical-scavenging properties towards a stable radical cation, ABTS, of Camelus dromedarius whey proteins (CWP) separated onto a cation-exchanger by fast protein liquid chromatography. The highest activities were found for CWP and fraction F1 mainly composed of α-lactalbumin. Fractions F2, F3 and F4 contained a mixture of lactoferrin, immunoglobulins G and probably camel whey basic protein (CWBP). These three fractions displayed low radical-scavenging activities. Lactoferrin was eluted almost pure in the last fraction (F5) but did not possess detectable radical-scavenging activity. The present results suggested that the cation-exchange chromatography is of great interest to yield, in a single step, whey protein fractions with various biological activities, i.e. a highly-enriched α-lactalbumin fraction displaying efficient antioxidant activity, a fraction (pool of F2-F4) mainly composed of heavy-chain immunoglobulins potentially interesting for human therapy and a fraction of pure lactoferrin having numerous biological activities such as antimicrobial and immunomodulating properties.

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Section: Investigation Of Radical-scavenging Activitycontrasting

confidence: 72%

Section: Investigation Of Radical-scavenging Activitymentioning

confidence: 80%

Section: Introductionmentioning

confidence: 99%

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Fast protein liquid chromatography of camel ?-lactalbumin fraction with radical scavenging activity

Halima

Jrad

Khorchani

et al. 2014

Emir. J. Food Agric

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“…Salami et al [100] studied the enzymatic digestibility and antioxidant activity of camel a-lactalbumin. Camel a-lactalbumin showed higher degrees of hydrolysis (digestibility) with both trypsin and chymotrypsin enzyme than bovine a-lactalbumin, but both proteins showed similar sensitivity to pepsin enzyme.…”

Section: Antioxidant Activitymentioning

confidence: 99%

Camel Milk: An Important Natural Adjuvant

et al. 2017

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One humped camel (Camelus dromedarius) breeds, indigenous to India, have been shown to have good genetic potential to produce milk. Camel milk not only is cost-effective in terms of feed conversion but also has additional advantage of longer lactation period and unique adaptation mechanisms for warm arid and semiarid regions. The key features of camel milk in comparison with other milk are low fat with high content of unsaturated and long-chain fatty acid. The proteins are rich in lactoferrin and lysozymes, but deficient in b-lactoglobulin. It has higher percentage of total salts, free calcium, protective proteins and vitamin C, and some of the microminerals, viz iron, copper and zinc. Physicochemical properties of camel milk are also unique and useful for food processing. The shelf life of raw camel milk is 8-9 h, which can be extended up to 18-20 h through activation of camel lactoperoxidase system. Heat stability of camel milk is shown to be highest at pH 6.8, and it ferments relatively slowly compared to the cattle milk. The camel milk is successfully processed for producing a variety of products, such as fermented milk ('lassi'), soft cheese, flavored milk and 'kulfee' (a kind of ice cream). Camel milk has been traditionally used in different regions of the world as natural adjuvant for managing a variety of human diseases.

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“…The spectrophotometric analysis of ABTS + radical-scavenging activity was determined according to method described by described by Salami et al (2009 …”

Section: Abts + Radical-scavenging Activitymentioning

confidence: 99%

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

Kumar

Chatli

Singh

et al. 2016

Dairy Sci. & Technol.

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The aim of this work was to investigate the enzymatic hydrolysis of whole casein from camel milk with proteolytic enzymes, viz. alcalase, α-chymotrypsin and papain, and to assess the antioxidant activity of hydrolysates. Casein powder was reconstituted (5% TS) and the selected enzymes were added at 1:100 (enzyme/substrate). Hydrolysis was carried out for 6 h at 55°C for alcalase and papain and 37°C for α-chymotrypsin, and samples were drawn at 2-h interval. The hydrolysates were analysed for pH, degree of hydrolysis (DH) and antioxidant activities, viz. 2, 2′-azinobis (3-ethylbenzthiazoline-6-sulphonic acid) (ABTS), 2, 2′-diphenyl-1-picrylhydrazyl (DPPH) and ferric reducing antioxidant power (FRAP) assay. The decrease in pH of the hydrolysates was observed with the progress of hydrolysis time, and as compared to alcalase, the rate of pH decrease was higher for α-chymotrypsin and papain. The DH increased significantly (P<0.05) up to 6 h on hydrolysis with alcalase and papain, whereas with chymotrypsinolysis, DH increased significantly (P<0.05) up to 4 h; thereafter, a non-significant increase was observed. The antioxidant activity assessed by ABTS, DPPH and FRAP assay increased significantly (P<0.05) with the increase in hydrolysis time as well as the degree of hydrolysis. The chymotrypsinolysis exhibited higher antioxidant activity as compared to alcalase and papain. The results obtained in this study suggested that camel milk casein could be used as an ingredient in nutraceuticals or health-oriented foods.

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Enzymatic digestion and antioxidant activity of the native and molten globule states of camel α-lactalbumin: Possible significance for use in infant formula

Cited by 86 publications

References 34 publications

Fast protein liquid chromatography of camel ?-lactalbumin fraction with radical scavenging activity

Fast protein liquid chromatography of camel ?-lactalbumin fraction with radical scavenging activity

Camel Milk: An Important Natural Adjuvant

Enzymatic hydrolysis of camel milk casein and its antioxidant properties

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