Conformational changes in bovine lactoferrin induced by slow or fast temperature increases

Schwarcz, Waleska Dias; Carnelocce, Lorena; Silva, Jerson L.; Oliveira, Andréa C.; Gonçalves, Rafael B.

doi:10.1515/bc.2008.116_bchm.just-accepted

Cited by 8 publications

(9 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…On the other hand, bLfcin has 10 hydrophobic residues in each peptide, some of them with high hydrophobic parameters, such as Ile, Val, and Leu. These hydrophobic residues may induce membrane disturbance by interacting with lipid bilayer, leading to membrane instability, permeability, and even rupture [12,[28][29][30][31][32]. Furthermore, nearly all the hydrophobic residues of bLfcin line up on one face of the peptide and most of the basic groups on the opposite face.…”

Section: Discussionmentioning

confidence: 99%

Effect of intramolecular disulfide bond of bovine lactoferricin on its molecular structure and antibacterial activity against Trueperella pyogenes separated from cow milk with mastitis

et al. 2020

View full text Add to dashboard Cite

Background Lactoferricin (Lfcin) is an antimicrobial activity center of lactoferrin, produced by hydrolysis from the N-terminal of lactoferrin. It was hypothesized that the intramolecular disulfide bond in Lfcin could affect its antibacterial function through influencing its molecular structure. To prove this hypothesis, bovine Lfcin (bLfcin) and its two derivatives, bLfcin with an intramolecular disulfate bond (bLfcin DB) and bLfcin with a mutation C36G (bLfcin C36G), were synthesized, purified, and identified. The circular dichroism spectra of the peptides were detected in solutions with different ionic and hydrophobic strength. The antibacterial activity of the peptides against Trueperella pyogenes, separated from cow milk with mastitis, were determined. Results The secondary structure of bLfcin DB showed more β-turn and less random coil than the other peptides in H2O, similar ratios of secondary structures with bLfcin and bLfcin C36G under ionic conditions, and close percentages of secondary structure with bLfcin under hydrophobic conditions. The synthetic peptides exhibited strong antimicrobial activity against T. pyogenes isolates, T. pyogenes ATCC 19,411, and E. coli ATCC 25,922. The antimicrobial activities of the three peptides were greater against T. pyogenes than against E. coli, and bLfcin DB exhibited higher antibacterial activity compared with its derivatives. Conclusions The intramolecular disulfide bond could change the molecular structure of bLfcin under alternative ionic strengths and hydrophobic effects, and the formation of the disulfide bond is beneficial to executing the antibacterial function of bLfcin.

show abstract

Section: Discussionmentioning

confidence: 99%

Effect of intramolecular disulfide bond of bovine lactoferricin on its molecular structure and antibacterial activity against Trueperella pyogenes separated from cow milk with mastitis

et al. 2020

View full text Add to dashboard Cite

show abstract

“…The applicant does not justify the claim that the production process used does not denature bovine lactoferrin (bLF). A recent study on this subject (Schwarcz et al, 2008) shows in particular that the pasteurisation of milk is likely to bring about changes to the tertiary structure of bLF, and thus to the properties linked thereto.…”

Section: Background As Provided By the European Commissionmentioning

confidence: 99%

Scientific Opinion on bovine lactoferrin

Products¹

2012

EFSA Journal

View full text Add to dashboard Cite

Following a request from the European Commission, the EFSA Panel on Dietetic Products, Nutrition and Allergies (NDA) was asked to carry out the additional assessment of "lactoferrin" as a food ingredient in the context of Regulation (EC) No 258/97 taking into account the comments and objections of a scientific nature raised by Member States. Bovine lactoferrin (bLF) is a protein that occurs naturally in cow"s milk. The applicant intends to market bLF as an ingredient for food supplements, infant and follow-on formulae, dietetic food for special medical purposes and sports nutrition, and for a variety of foods. For infants with an age of 0 -6 months, the applicant has estimated an intake of approximately 200 mg per kg bodyweight and 1.2 g bLF per day at the proposed use level. For adults, the mean and 95 th percentile daily intakes were calculated to be about 1.4 g and 3.4 g for an adult person. The toxicological information provided by the applicant included information from an in vitro genotoxicity study, a single dose study, a four week and a thirteen week oral repeated dose study in rats. The Panel notes that the estimated intake of "lactoferrin" for infants up to the age of one year of approximately 210 mg/kg bw per day would be around ten times lower than the highest dose (2,000 mg/kg bw per day) tested in the subchronic thirteen week rat study, which did not show adverse effects related to bLF. For adults above 19 years of age the proposed intake is approximately 100 times lower. This level of anticipated intake is considered a high intake scenario as opposed to a worst-case situation. The data provided suggest the absence of adverse effects of lactoferrin at the proposed levels of consumption. The Panel concludes that the novel food ingredient bLF is safe under the proposed uses and use levels. © European Food Safety Authority, 2012 KEY WORDSBovine lactoferrin, novel food, ingredient Bovine lactoferrin (bLF) is a protein that occurs naturally in cow"s milk. The applicant intends to market bLF in isolated and purified form. bLF is an iron-binding glycoprotein of approximately 77 kDa and consists of a single polypeptide chain of about 700 amino acids. The sequence homology between human and bLF is about 70 %. The tertiary structure of this glycoprotein has two ironbinding sites, giving it the capability to bind two Fe 3+ ions per molecule of protein. Batch testing confirmed that the product complies with the given specifications. bLF from skimmed milk is concentrated via ion exchange and is subsequently subjected to filtration steps. Ultimately the bLF is dried by means of spray drying. The applicant provided sufficient information regarding the specification, manufacture, composition and stability of bLF.The applicant intends to market bLF as an ingredient for food supplements, infant and follow-on formulae, dietetic food for special medical purposes and sports nutrition, and for foods such as nonalcoholic beverages, cakes and pastries, products derived from cheese, milk-based products, cold snacks...

show abstract

“…In particular, the ability of bovine lactoferrin to regulate bone cell growth has been well established (Cornish et al, 2004) and furthermore, oral feeding trials in ovariectomised rats (Blais, Malet, Mikogami, Martin-Rouas, & Tomé, 2009;Guo et al, 2009) and healthy postmenopausal women (Bharadwaj, Naidu, Betageri, Prasadarao, & Naidu, 2009) have indicated the potential of this bioactive protein in ameliorating bone loss during menopause. Although lactoferrin occurs naturally in milk, levels in bovine milk are relatively low (Cheng et al, 2008;Indyk & Filonzi, 2005) and the heat treatments required during manufacture and processing of dairy products are likely to cause denaturation of the protein and loss of bioactivity (Conesa et al, 2010;Schwarcz, Carnelocci, Silva, Oliveira, & Goncalves, 2008). Hence supplementation with commercially isolated non-denatured lactoferrin is an effective way to supply this bioactive ingredient.…”

Section: Introductionmentioning

confidence: 99%

“…As lactoferrin is a heat-sensitive protein and high temperatures such as those employed to pasteurise the yoghurt mix prior to fermentation are likely to result in the loss of bioactivity (Conesa et al, 2010;Schwarcz et al, 2008), it must be added either with the starter culture or following fermentation to avoid heat denaturation and loss of functionality. Although lactoferrin is a protein with broad spectrum antimicrobial properties (Jenssen & Hancock, 2009), studies have shown that it can act as a growth factor for certain probiotic Bifidobacterium strains (Rahman, Kim, Kumara, & Shimazaki, 2010) and additionally, it does not appear to have any growth inhibition activity against a variety of Lactobacillus strains (Tian, Maddox, Ferguson, & Shu, 2010).…”

Section: Introductionmentioning

confidence: 99%

Survival and bone-active properties of bovine lactoferrin supplemented into stirred yoghurt

Palmano

Ramos

Watson

et al. 2011

International Dairy Journal

View full text Add to dashboard Cite

Conformational changes in bovine lactoferrin induced by slow or fast temperature increases

Cited by 8 publications

References 22 publications

Effect of intramolecular disulfide bond of bovine lactoferricin on its molecular structure and antibacterial activity against Trueperella pyogenes separated from cow milk with mastitis

Effect of intramolecular disulfide bond of bovine lactoferricin on its molecular structure and antibacterial activity against Trueperella pyogenes separated from cow milk with mastitis

Scientific Opinion on bovine lactoferrin

Survival and bone-active properties of bovine lactoferrin supplemented into stirred yoghurt

Contact Info

Product

Resources

About