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

Animals ◽  
2020 ◽  
Vol 10 (2) ◽  
pp. 337 ◽  
Author(s):  
Ruixue Wang ◽  
Zhihao Han ◽  
Rimutu Ji ◽  
Yuchen Xiao ◽  
Rendalai Si ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Whey Proteins ◽  
Antimicrobial Activities ◽  
Camel Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Gel Chromatography ◽  
Milk Whey

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.

Proteomic Analysis of Cow, Yak, Buffalo, Goat and Camel Milk Whey Proteins: Quantitative Differential Expression Patterns

2013 ◽  
Vol 12 (4) ◽  
pp. 1660-1667 ◽  
Author(s):  
Yongxin Yang ◽  
Dengpan Bu ◽  
Xiaowei Zhao ◽  
Peng Sun ◽  
Jiaqi Wang ◽  
...  
Keyword(s):  
Differential Expression ◽  
Proteomic Analysis ◽  
Expression Patterns ◽  
Whey Proteins ◽  
Camel Milk ◽  
Milk Whey

scholarly journals THE EFFECT OF CAMEL MILK WHEY PROTEINS ON LACTIC ACID BACTERIA ISOLATED FROM CAMEL AND COW MILKS IN EGYPT: A COMPARATIVE STUDY.

2018 ◽  
Vol 6 (2) ◽  
pp. 986-998
Author(s):  
Mariam Mohammed ◽  
◽  
MarwaHEl Gendy ◽  
AidaS Salem ◽  
WafaiZA Mikhail ◽  
...  
Keyword(s):  
Lactic Acid ◽  
Lactic Acid Bacteria ◽  
Comparative Study ◽  
Whey Proteins ◽  
Camel Milk ◽  
Milk Whey

scholarly journals Chemical compositions, antioxidant and antimicrobial activities of Tubu (Pycnarrhena longifolia) leaves used as ingredient in traditional functional foods

Food Research ◽  
2020 ◽  
Vol 4 (3) ◽  
pp. 823-830
Author(s):  
N.K. Mohammed ◽  
B.J. Muhialdin ◽  
N.S. Masri ◽  
R. Sukor ◽  
F. Abd-El Aziem ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antioxidant Activity ◽  
Antibacterial Activity ◽  
Bioactive Compounds ◽  
Sugar Content ◽  
Antimicrobial Activities ◽  
Diffusion Method ◽  
Total Phenolic ◽  
Chemical Compositions ◽  
Food Ingredient

Tubu (Pycnarrhena longifolia) leaves are known as food enhancer and medicinal plant by several ethnics of Malaysia. The aims of the study were to determine the tubu leaves composition and biological activity including antioxidant and antibacterial. The mineral, sugar and amino acids were determined using HPLC, and bioactive compounds using GCMS. The antioxidant activity was evaluated by DPPH assay, and the antibacterial activity screened by disc diffusion method. The dry leaf compositions were 6.6% moisture, 11.6% ash, 7.0% crude protein, 15.7% crude fiber, 12.1% crude fat and carbohydrate 47%. A total of seven minerals were present in the methanol extract and the highest content was for iron (159.5 mg) and calcium (16.8 mg). The sugar profile showed high sugar content for glucose, sucrose, rhamnose, and fructose which was 8, 13, 7, and 20 mg/g, respectively. A total of sixteen amino acids was present in the tubu leaf extract, and seven bioactive compounds were identified by GC-MS/MS. The antioxidant activity was 87%, total phenolic compound content was 26.49 mg/mL and total flavonoid content was 13.39 mg/mL. Tubu leaves showed antibacterial activity towards Salmonella enterica serovar Typhimurium, Escherichia coli, Bacillus cereus and Staphylococcus aureus. This study showed that tubu leaves had rich sources of amino acids, minerals, sugars and bioactive compounds, potential to be a functional food ingredient.

scholarly journals Proteomics Analysis Reveals Altered Nutrients in the Whey Proteins of Dairy Cow Milk with Different Thermal Treatments

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4628
Author(s):  
Yangdong Zhang ◽  
Li Min ◽  
Sheng Zhang ◽  
Nan Zheng ◽  
Dagang Li ◽  
...  
Keyword(s):  
Thermal Treatment ◽  
Dairy Cow ◽  
Whey Proteins ◽  
High Heat ◽  
Cow Milk ◽  
Heat Sensitivity ◽  
Thermal Treatments ◽  
Milk Whey ◽  
Knowledge Based ◽  
Significant Difference

Thermal treatments of milk induce changes in the properties of milk whey proteins. The aim of this study was to investigate the specific changes related to nutrients in the whey proteins of dairy cow milk after pasteurization at 85 °C for 15 s or ultra-high temperature (UHT) at 135 °C for 15 s. A total of 223 whey proteins were confidently identified and quantified by TMT-based global discovery proteomics in this study. We found that UHT thermal treatment resulted in an increased abundance of 17 proteins, which appeared to show heat insensitivity. In contrast, 15 heat-sensitive proteins were decreased in abundance after UHT thermal treatment. Some of the heat-sensitive proteins were connected with the biological immune functionality, suggesting that UHT thermal treatment results in a partial loss of immune function in the whey proteins of dairy cow milk. The information reported here will considerably expand our knowledge about the degree of heat sensitivity in the whey proteins of dairy cow milk in response to different thermal treatments and offer a knowledge-based reference to aid in choosing dairy products. It is worth noting that the whey proteins (lactoperoxidase and lactoperoxidase) in milk that were significantly decreased by high heat treatment in a previous study (142 °C) showed no significant difference in the present study (135 °C). These results may imply that an appropriately reduced heating intensity of UHT retains the immunoactive proteins to the maximum extent possible.

Comparative Whey Proteome Profiling of Donkey Milk With Human and Cow Milk

2020 ◽  
Author(s):  
Xinhao Zhang ◽  
Guimiao Jiang ◽  
Chuanliang Ji ◽  
Haijing Li ◽  
Yantao Wang ◽  
...  
Keyword(s):  
Cholesterol Metabolism ◽  
Whey Proteins ◽  
Bioinformatic Analysis ◽  
Mass Spectrometry Analysis ◽  
Cow Milk ◽  
Label Free ◽  
Donkey Milk ◽  
Milk Whey ◽  
Spectrometry Analysis ◽  
Kegg Pathways

Abstract Background: Donkey milk (DM), similar to human milk (HM) in compositions, has been suggested as the best potential hypoallergenic replacement diet for babies suffering from cow milk (CM) protein allergens. Despite advances in proteomics technologies, studies of the DM whey proteome are relatively sparse. In this study, label-free mass spectrometry analysis was conducted to quantitatively identify the differentially expressed whey proteins (DEPs) in DM vs HM group and DM vs CM group. Results: In total, 249 and 418 DEPs were found in these two groups respectively. DEPs were then subjected to intensive bioinformatic analysis. Results revealed that the majority of DEPs participated in lipid metabolic process, regulation of cytokine production, chemical homeostasis and catabolic process. Kyoto Encyclopedia of Gene and Genomes (KEGG) pathways analysis found that these DEPs mainly participated in complement and coagulation cascades, and cholesterol metabolism. Conclusion: These results may provide valuable information in the composition of milk whey proteins in DM, HM and CM, especially for low abundant components, and expand our knowledge of different biological functions between DM and HM or CM.

scholarly journals The whey proteins of the milk of red deer (Cervus elaphus L.). A homologue of bovine β-lactoglobulin

1976 ◽  
Vol 153 (3) ◽  
pp. 647-655 ◽  
Author(s):  
E I McDougall ◽  
J C Stewart
Keyword(s):  
Cervus Elaphus ◽  
Red Deer ◽  
Whey Proteins ◽  
Major Constituent ◽  
Gel Chromatography ◽  
Starch Gel Electrophoresis ◽  
Milk Whey ◽  
Glutamic Acid Residue ◽  
Starch Gel ◽  
Β Lactoglobulin

1. The whey proteins from the milk of red deer are compared with those of cattle. Gel chromatography and electrophoresis showed a close similarity between the whey proteins of the two species in the size, mobility and relative amounts of the main constituents and in the changes in their relative amounts with time after parturition. 2. The major constituent of the deer whey was isolated. It appeared to be homologous with bovine β-lactoglobulin and had the following properties: m=-5.2×10(-9)m2-s-1-V-1 at 4 degrees C and pH 8.6; pI=5.17; S020, w =2.89S; v=0.748 ml/g; E1g/dl 1cm= 9.12 at 278 nm; deltan/c=1.794 × 10(-3)dl/g at 579 nm (all at 20 degrees C except m). Its molecular weight was that of a dimer with a subunit weight of 18 000. 3. Amino acid analyses of this protein, adjusted to lysine = 15 residues showed that it contains one more residue of aspartic acid, alanine and methionine and one less glutamic acid residue and two less leucine residues than bovine β-lactoglobulin A. 4. On starch-gel electrophoresis at pH 8.2, this protein migrated at the same rate as bovine β-lactoglobulin B, although its isoelectric point is close to that of the bovine A variant. Milk from three out of 27 hinds examined showed a variant. This migrated in starch gel at the same rate as the bovine A variant but had a more acid pI = 5.02. 5. The two species whose milk whey proteins are compared represent two different families of ruminants. The similarities found support the view that the milk whey proteins of the bovids are probably typical of the suborder as a whole.

scholarly journals Targeting Mycobacterium tuberculosis and Other Microbial Pathogens Using Improved Synthetic Antibacterial Peptides

2013 ◽  
Vol 57 (5) ◽  
pp. 2295-2303 ◽  
Author(s):  
Santiago Ramón-García ◽  
Ralf Mikut ◽  
Carol Ng ◽  
Serge Ruden ◽  
Rudolf Volkmer ◽  
...  
Keyword(s):  
Amino Acids ◽  
Mycobacterium Tuberculosis ◽  
Antimicrobial Peptides ◽  
Fungal Pathogens ◽  
Antimicrobial Activities ◽  
Microbial Pathogens ◽  
Cationic Antimicrobial Peptides ◽  
Content Type ◽  
Activity Spectrum ◽  
Low Cytotoxicity

ABSTRACTThe lack of effective therapies for treating tuberculosis (TB) is a global health problem. WhileMycobacterium tuberculosisis notoriously resistant to most available antibiotics, we identified synthetic short cationic antimicrobial peptides that were active at low micromolar concentrations (less than 10 μM). These small peptides (averaging 10 amino acids) had remarkably broad spectra of antimicrobial activities against both bacterial and fungal pathogens and an indication of low cytotoxicity. In addition, their antimicrobial activities displayed various degrees of species specificity that were not related to taxonomy. For example,Candida albicansandStaphylococcus aureuswere the best surrogates to predict peptide activity againstM. tuberculosis, whileMycobacterium smegmatiswas a poor surrogate. Principle component analysis of activity spectrum profiles identified unique features associated with activity againstM. tuberculosisthat reflect their distinctive amino acid composition; active peptides were more hydrophobic and cationic, reflecting increased tryptophan with compensating decreases in valine and other uncharged amino acids and increased lysine. These studies provide foundations for development of cationic antimicrobial peptides as potential new therapeutic agents for TB treatment.

Synthesis and antibacterial activity of trivalent ultrashort Arg-Trp-based antimicrobial peptides (AMPs)

MedChemComm ◽  
2015 ◽  
Vol 6 (2) ◽  
pp. 372-376 ◽  
Author(s):  
Barbara C. Hoffknecht ◽  
H. Bauke Albada ◽  
Marina Sturm ◽  
Pascal Prochnow ◽  
Julia E. Bandow ◽  
...  
Keyword(s):  
Amino Acids ◽  
Antibacterial Activity ◽  
Antimicrobial Peptides ◽  
Antimicrobial Agents ◽  
Multivalent Display

Multivalent display of identical ultrashort (only 2–3 amino acids long) antimicrobial peptides (AMPs) was used in order to create potential new antimicrobial agents.

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