Bioactive Compounds in Soybean Proteins and Its Applications in Food Systems

Sitohy, Mahmoud; Osman, Ali

doi:10.1007/698_2018_246

Cited by 10 publications

(13 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The storage of control minced meat increased both the pH value and the metmyoglobin level probably due to the increased bacterial activity [42]. Adding globulins to stored minced meat limited these changes understandably as a result of the low bacterial activities achieved by adding these protein fractions [19,37]. Further work will be necessary to study the mode of action of both 7S and 11S globulins of cowpea in details and to study the impacts of their modification chemically for their preservative effect for meat and other foods.…”

Section: Discussionmentioning

confidence: 99%

“…Many chemical additives are, therefore, used as food preservatives to promote food safety and extend food shelf life. The potential harmful effects associated with using chemical preservatives have switched on the search for safe natural bio-preservatives with considerable antimicrobial capacity, to be used in food industries [12,13,14,15,16,17,18,19,20].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Characterization and Antibacterial Activity of 7S and 11S Globulins Isolated from Cowpea Seed Protein

Abdel-Shafi

Al-Mohammadi²,

Osman

et al. 2019

Molecules

Self Cite

View full text Add to dashboard Cite

The present work was carried out to determine the characteristics and antibacterial activity of 7S and 11S globulins isolated from cowpea seed (Vigna unguiculata (L.) Walp.). The molecular mass of 7S globulin was demonstrated by SDS-PAGE bands to be of about 132, 129 and 95 kDa corresponding the α/, α and β subunits. The molecular mass of 11S globulin was demonstrated by SDS-PAGE bands to be existed between 28 and 52 kDa corresponding the basic and acidic subunits. The minimum inhibitory concentrations MICs of 7S and 11S globulins isolated from cowpea seed were determined against Gram positive bacteria viz: Listeria monocytogenes LMG 10470, Listeria ivanovii FLB 12, Staphylococcus aureus ATCC 25923 and Streptococcus pyogenes ATCC 19615, and Gram negative bacteria such as Klebsiella pneumonia ATCC 43816, Pseudomonas aeruginosa ATCC 26853, Escherichia coli ATCC 25922 and Salmonella ATCC 14028 using disc diffusion assay; they were showed to be in the range 10 to 200 µg/mL. Transmission electron microscope (TEM) examination of the protein-treated bacteria showed the antibacterial action of 11S globulin against S. typhimurium and P. aeruginosa was manifested by signs of cellular deformation, partial and complete lysis of cell components. Adding 11S globulin at both concentrations 50 and 100 µg/g to minced meat showed considerable decreases in bacterial counts of viable bacteria, psychrotrophs and coliforms compared to controls during 15 days storage at 4 °C, reflecting a promising perspective to use such globulin as a meat bio-preservative.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Characterization and Antibacterial Activity of 7S and 11S Globulins Isolated from Cowpea Seed Protein

Abdel-Shafi

Al-Mohammadi²,

Osman

et al. 2019

Molecules

Self Cite

View full text Add to dashboard Cite

show abstract

“…Natural antimicrobials from food sources are welcomed as food preservatives as they are not hazardous and have no side effects like those caused by synthetic ones [ 1 , 2 , 3 , 4 , 5 , 6 ]. These natural antimicrobials are quite promising for food bio-preservation to reduce the need for antibiotics, control of microbial spoilage process, and could kill the resistant variants of bacteria that can survive in foods and limit the occurrence of new food-borne disease outbreaks caused by pathogenic bacteria [ 7 , 8 , 9 , 10 , 11 , 12 ]. Natural extracts are compounds with a wide structural diversity, representing an important source of new chemical compounds with a possibly significant antibacterial action against food-borne pathogens with powerful action against multidrug-resistant bacteria [ 13 , 14 , 15 , 16 , 17 , 18 , 19 , 20 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

Powerful Antibacterial Peptides from Egg Albumin Hydrolysates

Al-Mohammadi¹,

Osman

Enan

et al. 2020

Antibiotics

Self Cite

View full text Add to dashboard Cite

Native egg albumin (NEA) was isolated from hen eggs and hydrolyzed by pepsin to produce hydrolyzed egg albumin (HEA). HEA was chemically characterized and screened for its antibacterial activity against 10 pathogenic bacteria (6 Gram (+) and 4 Gram (−)). The SDS-PAGE pattern of NEA showed molecular weights of hen egg albumin subunits ranging from 30 to 180 kDa. The highest intensive bands appeared at a molecular mass of about 50 and 97 kDa. Ultra-performance liquid chromatography (UPLC) of the peptic HEA revealed 44 peptides, 17 of them were dipeptides, and the other 27 fractions corresponded to bigger peptides (3–9 amino acids). The dipeptides and big peptides represented 26% and 74% of the total hydrolysate, respectively. The MIC of HEA was about 100 μg/L for Listeria monocytogenes, Bacillus cereus, Staphylococcus aureus, Salmonella typhimurium, Streptococcus pyogenes, and Klebsiella oxytoca and 150 μg/L for Pseudomonas aeruginosa, Bacillus subtilis, and Listeria ivanovii and 200 μg/L for Escherichia coli. L. monocytogenes was the most sensitive organism to HEA. Mixtures of HEA with antibiotics showed more significant antibacterial activity than individually using them. Transmission electron microscopy (TEM) revealed various signs of cellular deformation in the protein-treated bacteria. HEA may electrostatically and hydrophobically interact with the cell wall and cell membrane of the susceptible bacteria, engendering large pores and pore channels leading to cell wall and cell membrane disintegration. Higher cell permeability may, thus, occur, leading to cell emptiness, lysis, and finally death. Alternatively, no toxicity signs appeared when HEA was administrated to Wistar Albino rats as one single dose (2000, 5000 mg/kg body weight) or repeated daily dose (500 and 2500 mg/kg body weight/day) for 28 days to disclose the possible toxicity hazards. HEA did not produce any death.

show abstract

“…Using such natural seed proteins is promising perspective as it could avoid or limit the use of harmful chemical additives [6]. Seed globulins (SG) constitute most seed proteins within leguminous plants; they constitute over 51% of the total seed protein of cowpea, and over 53% of soybean seed protein.…”

Section: Introductionmentioning

confidence: 99%

“…The net positive charge of SG could be increased by methylation of their amino acid residues and in turn increase their antimicrobial activity [6]. Esterification is a successful way to produce modified seed globulins (MSG) with high antimicrobial activity.…”

Section: Introductionmentioning

confidence: 99%