2015
DOI: 10.1016/j.idairyj.2015.01.007
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Antibacterial activity of bovine milk lactoferrin and its hydrolysates prepared with pepsin, chymosin and microbial rennet against foodborne pathogen Listeria monocytogenes

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Cited by 32 publications
(11 citation statements)
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“…Al‐Nabulsi and others () reported the ability of lactoferrin in 0.2% peptone to reduce initial counts of Cronobacter spp by 4 log colony forming units (CFU)/mL of within a 4‐h incubation at 37 °C. Likewise, a 4 log cycle reduction of L. monocytogenes was achieved by at lactoferrin concentration of 1 mg/mL within 8 h of incubation at 37 °C (Ripolles and others ). The antimicrobial activity of this peptide is attributed either to its ability to limit microbial access to nutrients via iron chelation and/or to disturb the outer membrane of Gram‐negative bacteria (Gyawali and Ibrahim ).…”
Section: Natural Antimicrobial Agents For Food Preservationmentioning
confidence: 97%
“…Al‐Nabulsi and others () reported the ability of lactoferrin in 0.2% peptone to reduce initial counts of Cronobacter spp by 4 log colony forming units (CFU)/mL of within a 4‐h incubation at 37 °C. Likewise, a 4 log cycle reduction of L. monocytogenes was achieved by at lactoferrin concentration of 1 mg/mL within 8 h of incubation at 37 °C (Ripolles and others ). The antimicrobial activity of this peptide is attributed either to its ability to limit microbial access to nutrients via iron chelation and/or to disturb the outer membrane of Gram‐negative bacteria (Gyawali and Ibrahim ).…”
Section: Natural Antimicrobial Agents For Food Preservationmentioning
confidence: 97%
“…Milk lactoferrin concentration is affected by curding. Ripolles et al (2015) reported a reduction in antibacterial activity of bovine milk lactoferrin and its hydrolysates when different types of rennet were used, but lactoferrin is very resistant to heat treatments (Franco et al, 2018). Lactoperoxidase is not affected by curding according to Nandini and Rastogi (2011).…”
Section: Journal Of Dairy Researchmentioning
confidence: 99%
“…Proteolysis of bLF was performed with porcine pepsin (Sigma, USA) at a concentration of ω/ω of the substrate 3% at 37°C, pH 2.5 (Tomita et al, 1991;Ripolles et al, 2015). The reaction was stopped by heating the mixture for 15 minutes at 80°C.…”
Section: Proteolysis Of Blfmentioning
confidence: 99%
“…Already during the first hours of peptic proteolysis, accumulation of bLF peptides with a molecular weight of about 3 kDa was observed in the reaction mixture, with low molecular weight peptides mainly to cleave at the N-end of the molecule and to be represented by lactoferricins having high antimicrobial activity (Tomita et al, 1991;Ripolles et al, 2015). Further, the B. adolescentis B-1 peptides isolated from membrane were analyzed by electrophoresis, whereby their molecular weight was found to range 45-100 kDa.…”
Section: B Amentioning
confidence: 99%
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