A laboratory investigation of cow and camel whey proteins deposition under different heat treatments

Felfoul, Imène; Lopez, Christelle; Gaucheron, Frédéric; Attia, Hamadi; Ayadi, Mohamed Ali

doi:10.1016/j.fbp.2015.09.002

Cited by 35 publications

(18 citation statements)

References 27 publications

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“…The levels of heat-induced denaturation of α-la and BSA in bovine milk after HTST (4.23±1.37, and 2.70±0.31%, respectively) and UHT (51.06±2.11 and 5.37±1.46% respectively) treatments were considerably lower than those of their counterparts in heattreated CM. This finding is consistent with that observed by Felfoul et al (2015a) and Sagar et al (2016) who reported that camel α-la and SA were less heat stable and their temperatures of denaturation were lower than their bovine counterparts.…”

Section: Whey Proteins Denaturation Of Thermally and High-pressure Trsupporting

confidence: 93%

“…showed that heat treatment (121 °C for 15 min) of whole CM at its natural pH resulted in partial or complete protein precipitation indicating poor heat-stability; however, they demonstrated that the heat stability could be improved by increasing the milk pH to 7.0-7.2 and addition of κ-casein, EDTA or sodium phosphate. Furthermore, CM whey proteins were also reported to be more sensitive to heat treatments, with denaturation rates faster than those of bovine milk (Felfoul, Lopez, Gaucheron, Attia, & Ayadi, 2015a). Benabdelkamel et al (2017) indicated that heat treatment of CM whey at 98 °C for 60 min caused a significant denaturation of camel α-lactalbumin (α-la), lactoferrin (LF), and serum albumin (SA).…”

Section: Introductionmentioning

confidence: 99%

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Effects of industrial processing methods on camel skimmed milk properties

Omar

Harbourne

Oruña-Concha

2018

International Dairy Journal

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Effects of pasteurisation (high-temperature-short-time; HTST), ultra-high-temperature (UHT), and high-pressure (HP) treatments on some physical and chemical properties of camel milk (CM), including whey protein denaturation, colour change, casein micelle size, and rennet coagulation time (RCT), was investigated. UHT treatment caused the biggest colour change and highest whey protein denaturation in CM; in contrast, the effects of HP treatments on these properties were considerably less. Casein micelle size decreased after all treatments. The RCT of CM was significantly delayed and coagulum strength (G') decreased after HTST. HP treatment at 200 and 400 MPa increased the RCT of CM and the G' value was the highest after treatment at 200 MPa. Processing at 600 and 800 MPa inhibited coagulation of CM. The effects of both thermal and non-thermal treatments on many constituents and properties of CM were different from those on constituents and properties of bovine milk.

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Section: Whey Proteins Denaturation Of Thermally and High-pressure Trsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Effects of industrial processing methods on camel skimmed milk properties

Omar

Harbourne

Oruña-Concha

2018

International Dairy Journal

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“…Similar trend was observed for the casein content [39,57]. Konuspayeva et al [59] reported total protein content of camel milk varying from 2.1 to 4.9 percent.…”

Section: Proteinssupporting

confidence: 64%

“…Konuspayeva et al [59] reported total protein content of camel milk varying from 2.1 to 4.9 percent. Protein denaturation temperature for rennet and acid whey are reported as 73.8 and 60.50°C for camel and 70.5 and 63.9°C for cow [39]. Casein (CN) is the major protein (1.63-2.76%) in camel milk and constitutes about 52-87% of the total proteins.…”

Section: Proteinsmentioning

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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“…Sweet camel and bovine whey proteins (pH = 6.7) were obtained after a rennet enzyme coagulation (M. miehei, strength = 1:10,000, Laboratories Arrazi, Parachimic, Sfax, Tunisia) at 40°C as described by Felfoul, Lopez, Gaucheron, Attia, & Ayadi, 2015.…”

Section: Whey Proteins Preparationmentioning

confidence: 99%

Effect of pH on the physicochemical characteristics and the surface chemical composition of camel and bovine whey protein’s powders

et al. 2020

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A laboratory investigation of cow and camel whey proteins deposition under different heat treatments

Cited by 35 publications

References 27 publications

Effects of industrial processing methods on camel skimmed milk properties

Effects of industrial processing methods on camel skimmed milk properties

Camel Milk: An Important Natural Adjuvant

Effect of pH on the physicochemical characteristics and the surface chemical composition of camel and bovine whey protein’s powders

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