Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin

Pellegrini, Antonio; Dettling, Carmen; Thomas, Ursula; Hunziker, Peter

doi:10.1016/s0304-4165(01)00116-7

Cited by 199 publications

(122 citation statements)

References 23 publications

Supporting

Mentioning

103

Contrasting

Order By: Relevance

“…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

View full text Add to dashboard Cite

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.

show abstract

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

View full text Add to dashboard Cite

show abstract

“…The intact α-LA does not present antimicrobial activity [32]. In later research, Pellegrini et al, [33] Caseinomacropeptide (CMP) is the heterogeneous C-terminal fragment (f: 106-169) of bovine κ-casein composed of glycosylated and phosphorylated forms of different genetic variants. Malkoski et al, [34] showed that CMP presented inhibitory activity against the opportunistic pathogens of the oral cavity, Streptococcus mutans and Porphyromonas gingivalis and against Escherichia coli.…”

Section: Antimicrobial Activitymentioning

confidence: 99%

“…The intact α-LA does not present antimicrobial activity [32]. In later research, Pellegrini et al, [33] isolated, after action of trypsin on (β-LG), 4 polypeptides with bactericidal activity. The sequences of the 4 peptides were determined, as follows: Val-Ala-Gly-Thr-Trp-Tyr (f: 15-20); Ala-Ala-Ser-Asp-Ile-Ser-Leu-Leu-Asp-Gln-Ser-Ala-Pro-Leu-Arg (f: 25-40); Ile-Pro-Ala-Val-Phe-Lys (f: 78-83); Val-Leu-Val-Leu-AspThr-Asp-Tyr-Lys (f: 92-100).…”

mentioning

confidence: 99%

Food Proteins and Bioactive Peptides, Functional Diets

Sgarbieri¹,

Armadas²

2017

FSN

View full text Add to dashboard Cite

Throughout the second half of the last century and early this century the concept of the biological function of food proteins has changed significantly. While in the past the food proteins were regarded only as macronutrients capable of providing the amino acids to form the protein component of organs and tissues, also participating in the generation of metabolic energy for the normal functioning of living organisms, today it is known that certain proteins present in food, as well as fragments or peptides derived thereof, may participate in the general metabolism in a much more interactive manner, through bioactivities that go far beyond the nutritional functions that had been established by the end of the first half of the prior century.By making an analogy with the aeronautical activity we can say that in the past the food proteins functioned as black boxes holding numerous important pieces of information, which research and technology have only revealed, in part, in recent decades. In this period it Received: August 07, 2017; Accepted: September 12, 2017; Published: September 26, 2017 was found that certain proteins present in foods are naturally bioactive, and can be absorbed from the Gastrointestinal System (GIS) in their intact or slightly modified form and exercise specific bioactivities in the systemic metabolism [1], or, in addition, resist the action of digestive enzymes exercising different bioactivities in the gastrointestinal system [2]. Even more interesting were the findings that food proteins, of both plant and animal origin, contain, in their primary structures, specific amino acid sequences in their polypeptide chains, which when cleaved in the form of peptides by proteolytic enzymes or by specific chemical reagents may exercise diverse bioactivities that were latent in the original structure of the protein from which they originated.Bioactive peptides have been obtained from precursor proteins through the use of methodologies that have reached a high degree of sophistication and complexity, such as: (a) enzymatic hydrolysis by digestive enzymes; (b) proteolysis of the protein source by enzymes derived from microorganisms or plants; (c) fermentation process using culture with high proteolytic power and specificity. The bioactive potential of the peptides originating from the proteolysis of food proteins can be explored in the integral hydrolysates, produced in special conditions. However, in the current literature there are numerous research works and literature reviews emphasizing the importance of the isolation, purification, characterization, study of mechanisms and impact of these peptides on human health [3][4][5][6][7][8]. Production and Processing of Bioactive Peptides Derived from Food ProteinsA large number of plants and animals have been object of study as source of Bioactive Peptides (BAPs). Several studies were conducted, particularly with milk proteins [9,10], eggs [11,12], and muscle proteins from pigs [13], cattle [14], poultry [15], and fish [16]. BAPs have been obtained from...

show abstract

“…permeability of bacterial cells was determined using (13). Bacteria grown to logarithmic phase were adjusted to A 600 = 0.5 with TSB and mixed with two volumes of 10 mM sodium phosphate buffer, pH 7.4.…”

Section: Measurement Of Inner Membrane Permeabilization-the Inner Memmentioning

confidence: 99%

Characterization of the -Helix Region in Domain 3 of the Haemolytic Lectin CEL-III: Implications for Self-Oligomerization and Haemolytic Processes

Hisamatsu

Tsuda

Goda

et al. 2007

Journal of Biochemistry

View full text Add to dashboard Cite

SUMMARYCEL-III is a hemolytic lectin, which has two -trefoil domains (domains 1 and 2) and a -sheet-rich domain (domain 3). In domain 3 (residues 284-432), there is a hydrophobic region containing two helices (H8 and H9, residues 317-357) and a loop between them, in which alternate hydrophobic residues, especially Val residues, are present. To elucidate the role of the helix region in the hemolytic process, peptides corresponding to different parts of this region were synthesized and characterized. The peptides containing the sequence that corresponded to the loop and second helix (H9)showed the strongest antibacterial activity for Staphylococcus aureus and Bacillus subtilis through a marked permeabilization of the bacterial cell membrane. The recombinant glutathione S-transferase (GST)-fusion proteins containing domain 3 or the helix region peptide formed self-oligomers, whereas mutations in the alternate Val residues in the -helix region lead to decreased oligomerization ability of the fusion proteins. These results suggest that the -helix region, particularly its alternate Val residues are important for oligomerization of CEL-III in target cell membranes, which is also required for a subsequent hemolytic action. Keywords: antibacterial peptide, Ca 2+-dependent lectin, hemolysin, oligomerization, small-angle X-ray scattering 3 Abbreviations: CD, circular dichroism; SAXS, small-angle X-ray scattering; GST, glutathione S-transferase; TBS, Tris-buffered saline; TSB, tryptic soy broth; PBS, phosphate-buffered saline.4 CEL-III is one of the Ca 2+ -dependent, Gal/GalNAc-specific lectins isolated from the sea cucumber Cucumaria echinata (1). CEL-III exhibits strong hemolytic and cytotoxic activity through formation of oligomeric ion-permeable pores in the cell membrane, after binding to cell surface carbohydrate chains (2-4). From X-ray crystallographic analysis (5), CEL-III was found to consist of three domains (Fig. 1). Domains 1 and 2 are ricin-type (R-type) lectin domains (6), also known as trefoil domains, having carbohydrate-binding activity, while domain 3 has a novel structure composed of extended sheets and two helices positioned nearly perpendicular to the strands.Limited digestion of CEL-III with trypsin resulted in cleavage between these domains, followed by self-oligomerization of domain 3 fragments (7). This result suggested that domain 3 plays an important role in association of CEL-III molecules through interaction between its hydrophobic region, once separated from other domains. It seems that a conformational change induced by binding to carbohydrate chains on the target cell surface may lead to exposure of the hydrophobic surface of domain 3 of CEL-III.We have previously revealed that some 20-mer synthetic peptides corresponding to the helix region that spans -helices H8 and H9 (residues 320-354) of CEL-III ( Fig. 1) exhibited antibacterial activity toward two Gram-positive bacteria Staphylococcus aureus and Bacillus subtilis (8). This activity was assumed to be due to pert...

show abstract

Isolation and characterization of four bactericidal domains in the bovine β-lactoglobulin

Cited by 199 publications

References 23 publications

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

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

Food Proteins and Bioactive Peptides, Functional Diets

Characterization of the -Helix Region in Domain 3 of the Haemolytic Lectin CEL-III: Implications for Self-Oligomerization and Haemolytic Processes

Contact Info

Product

Resources

About