Antibacterial activity of papain hydrolysed camel whey and its fractions

Abdel-Hamid, Mahmoud; Goda, Hanan A.; Gobba, Cristian De; Jenssen, Håvard; Osman, Ali

doi:10.1016/j.idairyj.2016.04.004

Cited by 67 publications

(49 citation statements)

References 42 publications

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“…In general, most antimicrobial peptides are short (2-20 amino acids). Low mass peptides tend to have higher antibacterial activity than high mass peptides [35]. Table 2.…”

Section: Cawh-iii and Cowh-iii Gel Filtration Chromatographymentioning

confidence: 99%

Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions

Han

Xiao

et al. 2020

Animals

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Antibacterial peptides were isolated and purified from whey proteins of camel milk (CaW) and cow milk (CoW) and their antimicrobial activities were studied. The whey proteins were hydrolyzed using trypsin, and the degree of hydrolysis was identified by gel electrophoresis. The whey hydrolysate (WH) was purified using ultrafiltration and Dextran gel chromatography to obtain small peptides with antibacterial activity. The effect of the antimicrobial peptides on the morphology of bacterial strains was investigated using transmission electron microscopy. Their amino acid composition and antimicrobial activities were then determined. Polypeptides CaWH-III (<3 kDa) and CoWH-III (<3 kDa) had the strongest antibacterial activity. Both Fr.A2 (CaWH-Ⅲ’s fraction 2) and Fr.B1 (CoWH-Ⅲ’s fraction 1) had antibacterial effects toward Escherichia coli and Staphylococcus aureus, with minimum antimicrobial mass concentrations of 65 mg/mL and 130 mg/mL for Fr.A2, and 130 mg/mL and 130 mg/mL for Fr.B1, respectively. The highly active antimicrobial peptides had high amounts of alkaline amino acids (28.13% in camel milk Fr.A2 and 25.07% in the cow milk Fr.B1) and hydrophobic amino acids. (51.29% in camel milk Fr.A2 and 57.69% in the cow milk Fr.B1). This results showed that hydrolysis of CaW and CoW using trypsin produced a variety of effective antimicrobial peptides against selected pathogens, and the antibacterial activity of camel milk whey was slightly higher than that of cow milk whey.

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“…In general, most antimicrobial peptides are short (2-20 amino acids). Low mass peptides tend to have higher antibacterial activity than high mass peptides [35]. Table 2.…”

Section: Cawh-iii and Cowh-iii Gel Filtration Chromatographymentioning

confidence: 99%

Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions

Han

Xiao

et al. 2020

Animals

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“…• C for 5 min, and 10 µL of this mixture was loaded per well [27]. For Fourier transform infrared spectroscopy (FTIR analysis), WPC was prepared with potassium bromide [28].…”

Section: Preparation and Characterization Of Whey Protein Concentratementioning

confidence: 99%

The Effect of Dietary Replacement of Fish Meal with Whey Protein Concentrate on the Growth Performance, Fish Health, and Immune Status of Nile Tilapia Fingerlings, Oreochromis niloticus

Amer

Osman

Al-Gabri

et al. 2019

Animals

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The present study was conducted to assess the effect of replacing fish meal with whey protein concentrate (WPC) on the growth performance, histopathological condition of organs, economic efficiency, disease resistance to intraperitoneal inoculation of Aeromonas hydrophila, and the immune response of Oreochromis niloticus. The toxicity of WPC was tested by measuring the activity of caspase 3 as an indicator of cellular apoptosis. Oreochromis niloticus fingerlings with average initial weight 18.65 ± 0.05 gm/fish (n = 225) for a 10-week feeding trial. The fish were randomly allocated to five experimental groups, having five replacement percentages of fish meal with WPC: 0%, 13.8%, 27.7%, 41.6%, and 55.5% (WPC0, WPC13.8, WPC27.7, WPC41.6, and WPC55.5); zero percentage represented the control group. The results show that the fish fed WPC had the same growth performance as the WPC0. The total weight of bacterially challenged surviving fish increased linearly and quadratically (p ≤ 0.05) by increasing the replacement percentage of fish meal with WPC. The growth hormone, nitric oxide, IgM, complement 3, and lysozyme activity were seen to increase significantly in WPC27.7, especially after a bacterial challenge. The phagocytic percentage and phagocytic index increased significantly in WPC27.7, WPC41.6, and WPC55.5 groups. Histopathological examination of liver sections was badly affected by high replacement in WPC41.6–55.5. The activity of caspase 3 in the immunohistochemical stained sections of the intestine was increased significantly by increasing the inclusion level of WPC. Economically, the total return of the total surviving fish after the bacterial challenge was increased significantly by fish meal replacement with WPC. It could be concluded that WPC could replace the fish meal in Nile tilapia diets up to 27.7%, with improving the gut health, the total weight of survival fish, and immune status of fish challenged with A. hydrophila. High inclusion levels of WPC are not recommended in fish diets, since they negatively affected the intestinal and liver tissues and increased the level of cellular apoptosis, as indicated by the increased caspase 3 activity. Further researches are recommended to evaluate the effect of fish meal replacement with WPC on the histopathological examination of the kidney and to test the capacity of serum IgM to clot the bacteria used for the challenge.

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“…Milk caseins are an important source of AMP, and most AMP are derived from food proteins in milk (Florisa et al, 2003;Sibel Akalın, 2014). Some peptides from milk caseins demonstrating antimicrobial activity, reported in the literature, are released by enzymatic hydrolysis of plant sources such as protease extracted from the latex of Jacaratia corumbensis (Arruda et al, 2012) and papain (Abdel-Hamid et al, 2016). New protease-mediated hydrolysis of casein may release new AMP (Arruda et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption

Zhao

Shi

Wang

et al. 2020

Journal of Dairy Science

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This study aims to isolate the antimicrobial peptide (AMP) from buffalo casein hydrolyzed by Dregea sinensis Hemsl. protease. The AMP was isolated from hydrolysate by live bacteria adsorption, then analyzed using reversed-phase high-performance liquid chromatography, and the fraction with highest antimicrobial activity was identified by liquid chromatography-tandem MS. Further, we characterized the peptide in terms of its peptide sequence, structure, and antimicrobial activity. The results identified the AA sequence of the peptide as YLGYLEQLLRLK, which corresponds to residues 106 to 117 of bovine α S1-casein, and we named it BCp12. BCp12 displays α-helical structure, with high hydrophobic moments and net positive charge. BCp12 can inhibit the growth of indicator bacteria, with minimum inhibitory concentration values ranging from 0.8 to 1.6 mg/mL, and can induce low toxicity in mammalian cells. Antimicrobial activity of the BCp12 peptide remained stable under different salt concentrations but was sensitive to trypsin and high temperatures (121°C and above). The results support further research in the application of our newly generated AMP as an antimicrobial agent in the food industry and in food processing facilities.

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Antibacterial activity of papain hydrolysed camel whey and its fractions

Cited by 67 publications

References 42 publications

Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions

Antibacterial Activity of Trypsin-Hydrolyzed Camel and Cow Whey and Their Fractions

The Effect of Dietary Replacement of Fish Meal with Whey Protein Concentrate on the Growth Performance, Fish Health, and Immune Status of Nile Tilapia Fingerlings, Oreochromis niloticus

Characterization of a novel antimicrobial peptide from buffalo casein hydrolysate based on live bacteria adsorption

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