Dataset Information

Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin.

ABSTRACT: Lactoferrin is an 80 kDa bilobal, iron binding glycoprotein which is primarily antimicrobial in nature. The hydrolysis of lactoferrin by various proteases in the gut produces several functional fragments of lactoferrin which have varying molecular sizes and properties. Here, bovine lactoferrin has been hydrolyzed by trypsin, the major enzyme present in the gut, to produce three functional molecules of sizes approximately 21 kDa, 38 kDa and 45 kDa. The molecules have been purified using ion exchange and gel filtration chromatography and identified using N-terminal sequencing, which reveals that while the 21 kDa molecule corresponds to the N2 domain (21LF), the 38 kDa represents the whole C-lobe (38LF) and the 45 kDa is a portion of N1 domain of N-lobe attached to the C-lobe (45LF). The iron binding and release properties of 21LF, 38LF and 45LF have been studied and compared. The sequence and structure analysis of the portions of the excision sites of LF from various species have been done. The antibacterial properties of these three molecules against bacterial strains, Streptococcus pyogenes, Escherichia coli, Yersinia enterocolitica and Listeria monocytogenes were investigated. The antifungal action of the molecules was also evaluated against Candida albicans. This is the first report on the antimicrobial actions of the trypsin cleaved functional molecules of lactoferrin from any species.

SUBMITTER: Rastogi N

PROVIDER: S-EPMC3940724 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature

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Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin.

Rastogi Nilisha N Nagpal Nitish N Alam Hammad H Pandey Sadanand S Gautam Lovely L Sinha Mau M Shin Kouichirou K Manzoor Nikhat N Virdi Jugsharan S JS Kaur Punit P Sharma Sujata S Singh Tej P TP

PloS one 20140303 3

Lactoferrin is an 80 kDa bilobal, iron binding glycoprotein which is primarily antimicrobial in nature. The hydrolysis of lactoferrin by various proteases in the gut produces several functional fragments of lactoferrin which have varying molecular sizes and properties. Here, bovine lactoferrin has been hydrolyzed by trypsin, the major enzyme present in the gut, to produce three functional molecules of sizes approximately 21 kDa, 38 kDa and 45 kDa. The molecules have been purified using ion excha ...[more]

PMID: 24595088

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Project description:Pseudomonas fluorescens is implicated in food spoilage especially under cold storage, causing the increase of food waste and the reduction of environmental (and nutritional) sustainability. In food industry, Pseudomonas biofilm on pipe surfaces and facilities creates a persistent source of contamination and increases resistance to common disinfection strategies. Even though gene expression and protein pattern changes under environmental stimuli have been suggested, cellular mechanisms involved in biofilm production are poorly investigated for this species. In the present work, the cheese blue pigmenting P. fluorescens ITEM 17298 produced increased biofilm biomass and motility at 15 °C in comparison to 30 °C. Proteomic analysis revealed major differences of proteins involved in biofilm formation. In particular, at 15 °C we found increased amount of the c-di-GMP regulator PleD involved in motility as well as AlgB and the carbon storage regulator directly involved biofilm formation. Carbon metabolism, protein and fatty acid synthesis were also stimulated under cold incubation. Moreover, for the first time, enzymes correlated to indigoidine synthesis (blue pigment) were identified in the same condition. The differences in expression of regulatory proteins could therefore be the major determinant of the biofilm formation ability of P. fluorescens under refrigerated condition. Genomic and proteomic results also revealed virulence factors mostly detected at 30 °C. In order to counteract P. fluorescens persistence, this study also proposed a control strategy for biofilm development. Thus, a sub-lethal concentration of bovine lactoferrin hydrolysate (HLF) was assayed at both temperatures. Treatment caused a significant reduction in biofilm biomass, also confirmed by changes in proteome pattern. At each condition proteins involved regulatory functions and transcription factors were downregulated after HLF-treatment. Among these, at 15 °C we found that PleD was absent in treated samples, whilst negative regulators of alginate biosynthesis were detected; likewise, indigoidine related proteins were repressed. The cyclic-di-GMP-binding biofilm dispersal mediator was instead detected in all treated samples.

Dataset Information

Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin.

Publications

Preparation and antimicrobial action of three tryptic digested functional molecules of bovine lactoferrin.

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