Antimicrobial activity of recombinant human lactoferrin from Aspergillus awamori, human milk lactoferrin and their hydrolysates

Conesa, Celia; Rota, María C.; Pérez, María D.; Calvo, Miguel; Sánchez, Lourdes

doi:10.1007/s00217-008-0924-9

Cited by 9 publications

(6 citation statements)

References 32 publications

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“…1992). However, when we compared the effect of heat treatment on the antibacterial activity of human lactoferrin (Conesa et al. 2008) with that of bLF we observed that, although the highest treatment assayed (85°C, 10 min) destroyed completely the antibacterial activity of both proteins, the other treatments reduced it in some degree for the human protein, but did not have any effect on the bovine protein.…”

Section: Resultsmentioning

confidence: 96%

“…The thermal stability of human lactoferrin isolated from milk has been studied by differential scanning calorimetry (Mata et al 1998) and it was found to be more heat resistant than bLF when studied also by this technique (Sánchez et al 1992). However, when we compared the effect of heat treatment on the antibacterial activity of human lactoferrin (Conesa et al 2008) with that of bLF we observed that, although the highest treatment assayed (85°C, 10 min) destroyed completely the antibacterial activity of both proteins, the other treatments reduced it in some degree for the human protein, but did not have any effect on the bovine protein. This finding indicates that the antibacterial activity of bLF is better preserved than that of the human protein after heat treatment, in the same experimental conditions.…”

Section: R E S U Lt S a N D Discussionmentioning

confidence: 99%

“…Those peptides are located in the N‐terminus of lactoferrin without involving the iron‐binding sites and they are more active than the native lactoferrin itself (Van der Kraan et al. 2004; Conesa et al. 2008).…”

Section: Introductionmentioning

confidence: 99%

“…Two of these peptides are lactoferricin (Bellamy et al 1992a;1992b) and lactoferrampin (Van der Kraan et al 2004), both having cationic character. Those peptides are located in the N-terminus of lactoferrin without involving the iron-binding sites and they are more active than the native lactoferrin itself (Van der Kraan et al 2004;Conesa et al 2008). As they are relatively short peptides, positively charged and amphipatic, their main site of action has been proposed to be the cell membrane (Farnaud and Evans 2003).…”

Section: Introductionmentioning

confidence: 99%

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Effect of heat treatment on the antibacterial activity of bovine lactoferrin against three foodborne pathogens

Conesa

Rota

Castillo

et al. 2010

Int J of Dairy Tech

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The effect of different heat treatments on the antimicrobial activity of bovine lactoferrin against Escherichia coli O157:H7, Salmonella enteritidis and Listeria monocytogenes has been studied. We have observed that the heat treatments lower than 85°C for 10 min did not affect the antibacterial activity of the protein. Hydrolysates of bovine lactoferrin were found to be more active than the native protein against the three pathogens. Moreover, the antibacterial effect of bovine lactoferrin was also assayed in milk and whey, and although we found a reduction in the number of viable cells, this reduction was lower than in culture media.

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Section: Resultsmentioning

confidence: 96%

Section: R E S U Lt S a N D Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effect of heat treatment on the antibacterial activity of bovine lactoferrin against three foodborne pathogens

Conesa

Rota

Castillo

et al. 2010

Int J of Dairy Tech

Self Cite

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“…Antisera against LFb-nat were obtained in rabbits according to Conesa et al (2008b). The specific antibodies were obtained by immunoadsorption using LFb insolubilised in Sepharose-4B (Sigma, MO, USA).…”

Section: Methodsmentioning

confidence: 99%

Effect of high pressure on the structure and antibacterial activity of bovine lactoferrin treated in different media

Franco

Pérez

Castillo

et al. 2013

Journal of Dairy Research

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The effect of high-pressure treatment (400, 500 and 650 MPa) on the structure and activity of bovine lactoferrin in different iron-saturation forms has been studied by several techniques. The structural changes produced in lactoferrin by high-pressure were analysed by differential scanning calorimetry and fluorescence spectroscopy, and the immunoreactivity by ELISA. The effect of high-pressure was also studied on some biological properties of lactoferrin, such as iron binding capacity, retention of the bound iron, and antibacterial activity against Escherichia coli O157:H7. Results obtained indicate that treatment at 400 MPa does not substantially modify the conformation of lactoferrin, meanwhile treatments at 500 and 650 MPa greatly affect some of its properties. With respect to the antibacterial activity, the apo and native forms of lactoferrin maintain that activity against Esch. coli only after 400 MPa treatment.

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Antirotaviral potential of lactoferrin from different origin: effect of thermal and high pressure treatments

et al. 2018

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Rotaviral gastroenteritis causes a high rate of infant mortality and severe healthcare implications worldwide. Several studies have pointed out that human milk and dairy fractions, such as whey and buttermilk, possess antirotaviral activity. This activity has been mainly associated with glycoproteins, among them lactoferrin (LF). Thermal treatments are necessary to provide microbiological safety and extend the shelf life of milk products, though they may diminish their biological value. High hydrostatic pressure (HHP) treatment is a non-thermal method that causes lower degradation of food components than other treatments. Thus, the main objective of this study was to prove the antirotaviral activity of LFs from different origin and to evaluate the effect of several thermal and HHP treatments on that activity. LF exerted a high antirotaviral activity, regardless of its origin. Native LFs from bovine, ovine, swine and camel milk, and the human recombinant forms, at 1 mg/mL, showed neutralizing values in the range 87.5-98.6%, while human LF neutralized 58.2%. Iron saturation of bovine LF did not modify its antirotaviral activity. Results revealed interspecies differences in LFs heat susceptibility. Thus, pasteurization at 63 °C for 30 min led to a decrease of 60.1, 44.5, 87.1, 3.8 and 8% of neutralizing activity for human, bovine, swine, ovine and camel LFs, respectively. Pasteurization at 75 °C for 20 s was less harmful to the activity of LFs, with losses ranging from 0 to 13.8%. HHP treatment at 600 MPa for 15 min did not cause any significant decrease in the neutralizing activity of LFs.

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Antimicrobial activity of recombinant human lactoferrin from Aspergillus awamori, human milk lactoferrin and their hydrolysates

Cited by 9 publications

References 32 publications

Effect of heat treatment on the antibacterial activity of bovine lactoferrin against three foodborne pathogens

Effect of heat treatment on the antibacterial activity of bovine lactoferrin against three foodborne pathogens

Effect of high pressure on the structure and antibacterial activity of bovine lactoferrin treated in different media

Antirotaviral potential of lactoferrin from different origin: effect of thermal and high pressure treatments

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