Iron transport mechanism of lactoferrin and its application in food processing

FU, Jianing; YANG, Liu; TAN, Dehong; LIU, Ling

doi:10.1590/fst.121122

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Review Article • Food Sci. Technol 43 • 2023 • https://doi.org/10.1590/fst.121122 linkcopy

Iron transport mechanism of lactoferrin and its application in food processing

Authorship SCIMAGO INSTITUTIONS RANKINGS

Lactoferrin (LF) is a non-heme protein binding Fe³⁺ tightly and plays a role in regulating the absorption and metabolism of iron under physiological condition. The absorption of non-heme iron occurs in the duodenum. LF is incorporated as a functional factor of food products during food processing. In this review, we describe the structural and functional changes of LF due to thermal processing of food, as well as the metabolic processes of LF iron binding and release in vivo, which characterizes the value of LF as a food matrix from nutrition and biochemistry and provides a basis for the comprehensive utilization of LF in food.

Keywords:
lactoferrin; iron binding and release; lactoferrin digestion; lactoferrin function

Species	LF mg/mL	References
Human	1.0-7.0	(Rai et al., 2014)
Buffalo	0.03-0.81	(Giacinti et al., 2013)
Sheep	0.06-0.72	(Navarro et al., 2018)
Camel	0.02-2.1	(Azhar et al., 2020)
Equine	0.2-2.0	(Pieszka et al., 2016)
Bovine	0.03-0.2	(Liu et al., 2020a)
Goat	0.02-0.2	(Park, 2010)
Donkey	0.10-0.13	(Altomonte et al., 2019)

Functions	Categories	Mechanism/Results	References
Anti-cancer	Glioblastoma	bLF blocked the migration of human glioblastoma cell lines by reversing epithelial-to-mesenchymal transition-like processes and inhibiting the IL-6/STAT3 axis.	(Cutone et al., 2020a)
	Lung Adenocarcinoma	A novel human recombinant LF inhibited lung adenocarcinoma cell growth and migration with no cytotoxic effect on normal human epithelial cells.	(Olszewska et al., 2021)
	Breast Cancer	Lactoferricin B triggered mitochondrial membrane depolarization and elevated cytoplasmic calcium levels in MCF-7 cells.	(Guerra et al., 2019)
	Prostate Adenocarcinoma Cell	bLF inhibited proliferation, induced apoptosis, intracellular acidification and disrupted lysosomal acidification only in highly metastatic cancer cell lines, whereas BJ-5ta cells were insensitive to bLF.	(Guedes et al., 2018)
	Colon Cancer	bLF played a role in the protective mucus barrier that covers the intestinal epithelium.	(Tanaka et al., 2021)
Anti-viral	COVID-19	The binding of bLF to heparan sulfate proteoglycans blocked the attachment of the virus to the host cell, while HSPG mimetic heparin to antagonize the anti-viral activity of bLF.	(Hu et al., 2021)
Anti-viral	SARS-CoV-2	bLF interacts with pepsin during digestion and releases LF B17-41 with moderate anti-SARS-CoV-2 viral activity	(Wotring et al., 2022)
Anti-inflammatory	Acute Kidney Injury	Camel milk LF protected the kidney from 5-fluorouracil-induced inflammation and oxidative damage, while scavenging ROS, inhibiting MAPKs and NF-κB and activating the PI3K/Akt/eNOS pathway.	(Arab et al., 2018)
	Enteritis	In mouse model, by regulating the expression of PPAR-γ, PFKFB3 and NF-κB genes and proteins, apo-LF suppressed colonic mucosal inflammation and repaired mucosal damage.	(Fan et al., 2022)
	Arthritis and Air Pouch Edema	After internalization of LF into monocytes, LF in camel milk inhibited the activation of NF-κB, thereby inhibiting the production of pro-inflammatory cytokines.	(Arab et al., 2017)
Anti-bacterial	Burkholderia	A construct combining two antimicrobial structural domains of bLF lactoferrampin265-284 and lactoferricin17-30 resulted in disruption of the bacterial plasma membrane and subsequent leakage of intracellular nucleotides leading to cell death.	(Kanthawong et al., 2014)
	Vibrio Cholerae	bLF interacts directly with the negatively charged components of the microbial membrane, inducing changes in their permeability by dispersing them.	(Acosta-Smith et al., 2018)
	Neisseria Meningitidis	The C-lobe of hLF interacts with the bilobed outer membrane of Gram-negative bacteria at two different sites of lipoprotein, where binding of hLF prevents iron uptake or disrupts the protective membrane-bound lipoprotein against the cationic antimicrobial peptide.	(Ostan et al., 2017)
	Aflatoxin M1	LF resulted in a reduction in afm1-induced intestinal permeability, increased expression of claudin-3, ocludin and ZO-1 proteins, and repair of the damaged intestinal barrier.	(Gao et al., 2021)
	Cronobacter and Pseudomonas spp.	bLF inhibited the growth of sepsis-causing microorganisms in recombinant IMF and bacteria.	(Sawale et al., 2022)
	Salmonella enterica and E. coli O157:H7	The growth of E. coli O157:H7 was significantly reduced at LF concentrations greater than 14.05 mg/mL and the growth of S. enterica was reduced at LF concentrations equal to or greater than 112.5 mg/mL.	(Biernbaum et al., 2021)
Anti-parasitic	Amoebiasis	bLF-derived peptides were effective in resolving murine intestinal amoebiasis in vitro.	(Díaz-Godínez et al., 2019)
Osteogenesis	Osteogenic Factor	By activating Smad2/3 and p38 MAPK, bLF enhanced osteoblast differentiation from MSCs, resulting in increased transcriptional activity of Runx2. bLF treatment enhanced osteoblast differentiation and mineralized nodule formation, as well as the repair of bone defects in vitro.	(Inubushi et al., 2020)
Enzyme activity	DNA Binding	LF has a sequence similar to ribonuclease A and has DNA-binding properties that allow it to act in the transcriptional activation of specific DNA sequences and also as a mediator of signal transduction.	(Brandl et al., 2010; García-Montoya et al., 2012)
Nerve Function Regulation	Neural Development and Cognition	LF improved neurodevelopment, cognition, and memory in piglets through upregulation of brain-derived neurotrophic factor signaling pathways.	(Chen et al., 2015)

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