Fractionation of sheep cheese whey by a scalable method to sequentially isolate bioactive proteins

Pilbrow, Jodi; Bekhit, Alaa El‐Din A.; Carne, Alan

doi:10.1016/j.foodchem.2016.02.065

Cited by 12 publications

(5 citation statements)

References 34 publications

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“…The molecular weights (MWs) of the solubilized keratin extracts were determined using one-dimensional sodium dodecyl sulfate polyacrylamide gel electrophoresis (1D SDS-PAGE) following the method previously described. 22 The diameters of the protein particles in the solution were calculated using Zetasizer Nano-ZS using a protein concentration of 1 mg mL −1 in distilled water. Determination of the dynamic viscosity of keratin extracts was performed using a Rheometer (HAAKE RheoStress 1, Thermo Fisher Scientific, Waltham, MA USA) at 20°C, using a Z34 DIN Ti sensor with 34 mm diameter.…”

Section: Sample Characterizationmentioning

confidence: 99%

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

Shavandi

Bekhit

Carne

et al. 2016

Journal of Bioactive and Compatible Polymers

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This study investigated some physicochemical properties of keratin extracted from Merino wool using five chemical extraction methods: alkali hydrolysis, sulfitolysis, reduction, oxidation, and extraction using ionic liquid. The ionic liquid method produced the highest protein yield (95%), followed by sulfitolysis method (89%), while the highest extraction yield was obtained with the reduction method (54%). The lowest yield was obtained with the oxidation method (6%). The oxidation extract contained higher molecular weight (>40 kDa) protein components, whereas the alkali hydrolysis extract contained protein material of <10 kDa. The sulfitolysis, reduction, and ionic liquid extracts contained various protein components between 3.5 and 60 kDa. Keratin obtained from various extraction methods had different yield, morphology, and physicochemical properties. None of the samples were toxic to L929 fibroblast cells up to a concentration of 2.5 mg/mL. Apart from the alkali hydrolysis extract, all other keratin extracts (reduction, sulfitolysis, ionic liquid, and oxidation) showed Fourier transform infrared adsorption peaks attributed to the sulfitolysis–oxidation stretching vibrations of cysteine-S-sulfonated residues, with the oxidation extract showing the highest content of cysteine-S-sulfonated residues. This study indicates that the properties of the keratin extract obtained vary depending on the extraction method used, which has implications for use in structural biomaterial applications.

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Section: Sample Characterizationmentioning

confidence: 99%

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

Shavandi

Bekhit

Carne

et al. 2016

Journal of Bioactive and Compatible Polymers

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“…Lf was enriched from deer milk using a sequential ion exchange chromatography method [15]. Deer milk sweet whey was prepared by adding 1 mL renin solution (Renco, Eltham, New Zealand) per litre of deer milk, incubating at 37 • C, 1 h, and the clarified sweet whey fraction was obtained by centrifuging at 10,000× g, 15 min.…”

Section: Purification Of Deer Lactoferrin By Fast Protein Liquid Chromatographymentioning

confidence: 99%

Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin

Wang

Morton

Bekhit

et al. 2021

Foods

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Although the bioactivities of bovine lactoferrin have been extensively investigated, little is known about deer milk lactoferrin bioactivity and its amino acid sequence. This research investigated the amino acid sequence of deer lactoferrin and the antimicrobial activities of two lactoferrin-encrypted peptides; lactoferricin (Lfcin) and lactoferrampin (Lfampin). Deer lactoferrin was found to have a molecular weight of 77.1 kDa and an isoelectric point of 7.99, which are similar to that of bovine lactoferrin, 78 kDa and pI 7.9. Deer lactoferrin contains 707 amino acids, one amino acid less than bovine lactoferrin, and has 92% homology with bovine lactoferrin. Deer lactoferricin exhibited strong antimicrobial activity against E. coli American Type Culture Collection (ATCC) 25922 and L. acidophilus ATCC 4356. The antimicrobial activities of deer and bovine Lfcin and Lfampin were compared. Based on MIC, deer Lfcin was found to be a more effective inhibitor of L. acidophilus ATCC 4356 than bovine Lfcin, but bovine Lfcin and Lfampin were more effective against E. coli ATCC 25922 than deer Lfcin and Lfampin. The deer Lfcin sequence differed at seven amino acids from bovine Lfcin and this decreased the net positive charge and increased the hydrophobicity. Deer Lfampin contained two differences in amino acid sequence compared to bovine Lfampin which decreased the net positive charge. These amino acid sequence differences likely account for differences in antibacterial activity. Positive charge and hydrophobic residues provide the amphipathic character of these helical peptides, and are considered important for binding of antimicrobial peptides. In silico modelling of deer Lfcin indicated an identical α-helical structure compared to bovine Lfcin.

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“…This bioactivity is observed with different commercial whey products (Whey Protein Isolate, Whey Protein Concentrate), is relatively resistant to processing method, and is increased by enzymatic hydrolysis [5]. The absence of phenylalanine in glycol (caseino)macropeptide in whey protein makes it attractive for use in food formulations for phenylketonuriacs [6].…”

Section: Nutrition Value Of Wheymentioning

confidence: 99%

Applications of Whey as A Valuable Ingredient in Food Industry

Chandrajith

2018

JDVS

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Many scientific researches have been carried out on utilization of whey which is considered as a waste in dairy industry. It is hazardous to dispose whey directly in to the environment because several toxic substances are formed during decomposition of whey and it can cause several harmful consequences on the environment. Whey protein fraction consists of many useful nutrients that can be benefitial to human nutrition. This study presents the possible applications on whey in food industry and other fields and the possibility to recycle the whey incorporating them in to secondary dairy products.

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Fractionation of sheep cheese whey by a scalable method to sequentially isolate bioactive proteins

Cited by 12 publications

References 34 publications

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

Evaluation of keratin extraction from wool by chemical methods for bio-polymer application

Amino Acid Sequences of Lactoferrin from Red Deer (Cervus elaphus) Milk and Antimicrobial Activity of Its Derived Peptides Lactoferricin and Lactoferrampin

Applications of Whey as A Valuable Ingredient in Food Industry

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