Isolation and identification of three bactericidal domains in the bovine Î±-lactalbumin molecule

Pellegrini, Antonio; Thomas, Ursula; Bramaz, Nadine; Hunziker, Peter; Fellenberg, R. von

doi:10.1016/s0304-4165(98)00165-2

Cited by 238 publications

(158 citation statements)

References 27 publications

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“…The observed inhibitory action of the yoghurt, casein fraction and soluble protein fraction contrasted to inactivity of the sheep milk proteins may be due to the fact that the small peptide fragments can have more feasible access into the microbial membranes than the bigger-sized intact protein, and is in agreement with the conclusion of Schanbacher et al,(1998). Alternatively, some released peptides may have particular peptide primary structure more suited to the antimicrobial action; it may have higher content of positively charged amino acid residues, hydrophobic amino acid residues or some amino acid residues of particular importance for the antimicrobial action (Pellegrini et al, 1999(Pellegrini et al, , 2003. Anti-Staphyloccocus aureus activity of sheep yoghurt Fig.…”

Section: Results and Discussion Turbidity-based Bacterial Growthsupporting

confidence: 57%

Antimicrobial Activity of Sheep Yoghurt Prepared by Different Commercial Starter Strains

2009

Alexandria Science Exchange Journal: An International Quarterly

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The antimicrobial activities of sheep milk yoghurt prepared by different starter strains were evaluated against different pathogenic microbial strains using different techniques. Sheep yoghurt prepared with LAB starters YC-183 and probiotic starter ABT-3, manifested anti-Staphylococcus aureus activities. Most antimicrobial activities were associated with yoghurt soluble proteins fraction and originating from high molecular weight peptide fragments (more than 3000 Dalton) if the milk yoghurt was pretreated at 85?C / 10 min, but from low molecular weight peptides (lower than 3000 Dalton) if the milk used was pretreated at 96?C/ 5 min. Yoghurt prepared by all starter cultures exhibited antimicrobial activity against E.coli HB101. This activity was more pronounced in the casein fraction of the yoghurt prepared after heating at 96?C/5 min especially those prepared with ABT-3 culture. Comparable or slightly lower activities were associated with soluble protein fractions separated from different starter-yoghurt prepared from sheep milk preheated at 85?C/10 min which loosed their activities after ultrafiltration through 3000 Da membrane. This inhibitory action was particularly evident against Staphylococcus aureus and E. coli HB101. An antibacterial peptide against E. coli which generated from -casein by the proteolytic system of starter culture of yoghurt was isolated and this peptide has a molecular weight 4.6KDa.

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Section: Results and Discussion Turbidity-based Bacterial Growthsupporting

confidence: 57%

Antimicrobial Activity of Sheep Yoghurt Prepared by Different Commercial Starter Strains

2009

Alexandria Science Exchange Journal: An International Quarterly

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“…Many AMPs are generated from different species milk proteins after degradation whether by enzymes produced by animals (gastro-intestinal enzymes), plants or micro-organisms or during manufacturing of dairy derived products but not from colostrum. Several antimicrobial peptides derived from milk proteins' digestion are well known now as fragments LTD1 (1-5) (Pellegrini et al, 1999), bovine β-Lactoglobulin (Pellegrini et al, 2001), bovine αS1-Casein (Recio and Visser, 1999), αS2-Caseine, κ-Caseine, human κ-Caseine, bovine lactoferrin (Bellamy et al, 1992), human lactoferrin (Wakabayashi et al, 2006) and caprine lactoferrin (Recio and Visser, 2000). However, no information is available regarding peptides derived from proteins of camel milk and colostrum.…”

Section: Introductionmentioning

confidence: 99%

Camel colostrum: Nutritional composition and improvement of the antimicrobial activity after enzymatic hydrolysis

Jrad

Oulahal

Adt

et al. 2015

Emir. J. Food Agric

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Camel colostrum collected within 24 h after parturition was analyzed for physicochemical and microbiological composition. The average contents of fats, dry matter, mineral matter and proteins were 1.71±0. 51, 199.55±16.93, 9.75±0.5 and 143.42±36.42 gL -1 , respectively. Microbiological analysis of colostrum samples showed richness in yeasts and Lactic acid bacteria and absence of coliforms. The good microbial quality of camel colostrum is due to a number of antimicrobial molecules such as immunoglobulins and lactoferrin. The antimicrobial activity was evaluated against the pathogens Bacillus cereus, Staphylococcus aureus, Enterococcus faecium and Pseudomonas aeruginosa. At concentration of 20 g L -1 , colostrum caused an important inhibition of growth of all tested bacteria. It therefore seemed interesting to assess whether the compounds inhibit the growth of tested strains present in camel colostrum are resisting to the action of digestive enzymes. An in vitro hydrolysis by pepsin and pancreatin was then conducted. Hydrolyzed camel colostrum was still active against all pathogenic strains with inhibition rate ranging from 15.8% to 24.18%. This finding highlights the presence of antimicrobial fragments/peptides released during proteolytic hydrolysis that may contribute to the antimicrobial activity in camel colostrum and play a significant role in the host defence system.

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“…α-LA is a small, acidic, molten-globule, cation-binding milk protein, which has several important biological functions, such as lactose synthesis and Ca 2+ binding (Lonnerdal and Glazier, 1985;Bleck et al, 1998). In addition, α-LA has been linked to antimicrobial activity (Pellegrini et al, 1999;Kilara and Panyam, 2003), reduction of stress (Markus et al, 2000), immunomodulation (Brody, 2000;Cross and Gill, 2000), regulation of cell growth (Sternhagen and Allen, 2001), antiulcer activity (Matsumoto et al, 2001), and antihypertensive activity (Fitzgerald et al, 2004). However, its most important function is related to milk productivity in cows (Bleck and Bremel, 1993).…”

Section: Introductionmentioning

confidence: 99%

Association between a polymorphism of the α-lactalbumin gene and milk production traits in Chinese Holstein cows

Zhang¹,

Dong²

2013

Genet. Mol. Res.

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ABSTRACT. The traits particularly important for milk production include milk yield, protein percentage, fat percentage, and the somatic cell score. Alpha-lactalbumin (α-LA) is an important whey protein of cow milk, and is also present in the milk of many other mammalian species. In this study, we analyzed the genetic polymorphisms of the α-LA gene and their relationship to milk production traits (milk yield, protein percentage, fat percentage, and somatic cell score) in Chinese Holstein cows. The goal of this study was to contribute further molecular genetic information related to dairy cattle, to determine the molecular markers that are most closely linked with milk production traits, and to provide a scientific basis for the improvement of economically relevant traits in cows. Fluorescence-based conformation-sensitive gel electrophoresis, DNA sequencing, and ligation detection reaction techniques were used to analyze genetic variations of the α-LA gene (5ꞌ-UTR, exons 1, 2, 3, 4, and 3ꞌ-UTR) in 923 Chinese Holstein cows. One novel single nucleotide polymorphism (SNP), α-LA2516, was identified in exon 4 of the α-LA gene. Allele frequencies were as follows: T 0.674, C 0.326. Association analysis revealed that α-LA2516 was not associated with milk yield, These findings suggest that the SNP α-LA2516 in the α-LA gene likely does not have potential as a molecular marker for milk production traits in Chinese Holstein cows.

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Isolation and identification of three bactericidal domains in the bovine Î±-lactalbumin molecule

Cited by 238 publications

References 27 publications

Antimicrobial Activity of Sheep Yoghurt Prepared by Different Commercial Starter Strains

Antimicrobial Activity of Sheep Yoghurt Prepared by Different Commercial Starter Strains

Camel colostrum: Nutritional composition and improvement of the antimicrobial activity after enzymatic hydrolysis

Association between a polymorphism of the α-lactalbumin gene and milk production traits in Chinese Holstein cows

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