• Journal of Animal Science and Technology
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• v.48 no.4
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• pp.595-602
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• 2006

The purpose of this study is to demonstrate antimicrobial activities of the lactoferrin and its peptic hydrolysates obtained from the colostrums of Hanwoo(Korean native cattle) and Holstein cattle. In the measurement of antimicrobial activity to E. coli O111 and other microorganisms, bovine lactoferrin showed a higher antimicrobial activity than that of Hanwoo cow's lactoferrin . The minimal inhibitory concentration (MIC) of lactoferrin against E. coli O111 was exhibited 1.5mg/ml(Holstein) and 2.75mg/ml (Hanwoo). The same result was also observed between bovine lactoferrin hydrolysate (0.12mg/ml) and Hanwoo cow's lactoferrin hydrolysate (0.25mg/ml). In addition of lysozyme, antimicrobial activity of lactoferrin was increased.

• 한국유가공학회:학술대회논문집
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• 2002.04a
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• pp.37-42
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• 2002

Lactoferrin is an iron-binding glycoprotein and its bacteriostatic and bactericidal effects on Gram-positive and Gram-negative bacteria have been well-known. However, certain kind of lactic acid bacteria are resistant against its antibacterial effects. Moreover, it is reported that lactoferrin promotes the growth of bifidobacteria by in vitro and in vivo experiments. In this experiment, lactoferrin-binding protein was found both in the membrane and cytosolic franctions of Bifidobacterium. Bifidobacterium was grown in anaerobic conditions in MRS broth containing cysteine, gathered by centrifugation and processed by sonication. The lactoferrin-binding proteins on the PVDF-membrane transferred after SDS-PAGE were detected by far-western method using biotinylated lactoferrin and streptavidin-labeled horse radish peroxidase. Observation in growth effects of lactoferrin on Bifidobacterium suggested that there is a relation between the presence of lactoferrin-binding proteins on the cells and their growth.

• Food Science of Animal Resources
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• v.20 no.2
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• pp.125-132
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• 2000

Lactoferrin was isolated from the colostrum of Korean native cow by using several purification steps such as batch extraction, ion exchange chromatography, gel filtration chromatography and affinity chromatography. Other whey protein components that having similar molecular weight and affinity to lactoferrin were gradually removed from crude Korean native cow's lactoferrin during the purification steps. The amount of lactoferrin collected from a liter of Korean native cow's colostrum was 65mg and the recovery rate was 29.4%. The molecular weight of the purified Korean native cow's lactoferrin was estimated approximately 81,000dalton.

• Journal of Dairy Science and Biotechnology
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• v.37 no.2
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• pp.129-135
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• 2019

This study investigated the effects of heat-treated and non-heat-treated bovine lactoferrin on the growth of Lactococcus lactis subsp. cremoris JCM 20076. The addition of heat-treated and non-heat-treated bovine lactoferrin in adjusted MRS medium stimulated the growth of Lc. cremoris JCM 20076. Heat-treated bovine lactoferrin had a greater impact on the growth of Lc. cremoris JCM 20076 compared to that with non-heat-treated bovine lactoferrin. Bovine lactoferrin heated at $65^{\circ}C$ for 30 min stimulated the growth of the bacteria more than that heated at $80^{\circ}C$ for 5 min. Furthermore, the growth of Lc. cremoris JCM 20076 increased substantially with heat-treated bovine lactoferrin at a concentration of 1 mg/mL.

• Journal of the Korean Applied Science and Technology
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• v.30 no.4
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• pp.779-789
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• 2013

This study aimed to investigate the emulsifying properties of bovine lactoferrin in food emulsion system. First, lactoferrin solution was prepared to study its surface activities, such as surface adsorption characteristics and ${\zeta}$-potential. Second, some physicochemical properties of lactoferrin emulsion which resulted from variations of environmental conditions (i.e., pH or NaCl addition) were determined. As for surface adsorption characteristics evaluated by surface tension, it was decreased with increasing lactoferrin concentration in solution ($1{\times}10^{-5}{\rightarrow}0.2wt%$) and showed a plateau (${\fallingdotseq}44$mN/m) above 0.01 wt%. It was also changed with pH and the minimum value of 53.8 mM/m was observed at pI of lactoferrin. This was related to changes in ${\zeta}$-potential of the lactoferrin solution with respect to pH. Fat globule size of lactoferrin emulsion was decreased with increasing lactoferrin concentration and a stable emulsion was formed above 0.5 wt% lactoferrin in emulsion with fat globule size $d_{32}$ of ca. 0.33 ${\mu}m$ as confirmed by creaming stability experiment (i.e., Turbiscan). As with surface tension, fat globule size of lactoferrin emulsion also changed with pH and showed a maximum value at pI. As evaluated by Turbiscan, in the presence of NaCl, the lactoferrin emulsion showed instability in particular above 10 mM.

• Journal of Dairy Science and Biotechnology
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• v.27 no.1
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• pp.19-28
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• 2009

Lactoferrin was first identified 60 years ago as a "red protein" in bovine milk. Lactoferrin, one of the transferrin family proteins, is an iron-binding glycoprotein found in milk and various mucosal secretions; it is also released from activated neutrophils. Human lactoferrin has a molecular weight of 82.4 kDa and is composed of 702 or 692 amino acid residues. Bovine lactoferrin has a molecular weight of 83.1 kDa and is composed of 689 amino acid residues. Both lactoferrin and transferrin have the ability to bind two $Fe^{3+}$ ions, together with two ${CO_3}^{2-}$ ions with extremely high affinity; these proteins also have the ability to release this iron at low pH levels. The polypeptide chain in lactoferrin is folded into two globular lobes, representing the N-terminal and C-terminal halves. Both lobes have similar folding and 40% sequence identity. This protein is capable of multiple functions as described in various review papers, including antimicrobial, antiviral, antiinflammatory, anticancer, antioxidant, and cell growth-promoting activities. Lactoferrin also exhibits immunomodulating effects and plays an active role in the regulation of myelopoiesis and the inhibition of bacterial translocation.

• Korean Journal of Head & Neck Oncology
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• v.9 no.1
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• pp.74-87
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• 1993

Immunohistochemical studies on S-100 protein and lactoferrin were carried out to evaluate the existence and distribution pattern of S-100 protein and lactoferrin positive cells in salivary gland tumors. The specimens used were 25 cases of pleomorphic adenoma, 2 cases of monomorphic adenoma, 2 cases of mucoepidermoid tumor, 2 cases of acinic cell tumor, 3 cases of adenoid cystic carcinoma and 2 cases of adenocarcinoma occured in parotid and submandibular salivary gland. ABC kits(Dako corp. Copenhagen. Denmark) for S-100 protein and lactoferrin were used. The results obtained were summarized as follows: In the normal salivary gland. positive immunoreaction for S-100 protein was observed in myoepithelial cells of acini and intercalated ducts. Positive immunoreaction for lactoferrin was observed in serous acinic cells, epithelial cells of intercalated ducts, and excretory material in the ductal lumina. In the pleomorphic and monomorphic adenomas. most of tumor cells were positive for S-100 protein, while luminal tumor cells in gland-like or duct-like structures were rarely positive for lactoferrin. In mucoepidermoid tumor, most of squamous cells and a few of intermediate cells were positive for S-100 protein, but all of tumor cells were negative for lactoferrin. In acinic cell tumor, most of tumor cells were positive for lactoferrin, but all of tumor cells were negative for S-100 protein. In adenoid cystic carcinoma, basaloid tumor cells in trabecular structure were focally positive for S-100 protein. and in adenocarcinoma, many of tumor cells were posivive for both S-100 protein and lactoferrin. Thus, according to the embryonic stage of the development of the tumor cell origin, it was possible to classify the salivary gland tumor as followings: mucoepidermoid carcinoma which originated from the earliest stage, acinic cell tumor which originated from the end stage. Between these two extremes, there were pleomorphic adenoma, adenoid cystic carcinoma and adenocarcinoma which originated in the middle stage of the development of .the salivary glands. Based on the above results, it can be stated that S-100 protein is demonstrated in tumor cells orginated from myoepithelial cells and lactoferrin in glandular differentiated tumor cells.

• Journal of Veterinary Clinics
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• v.12 no.1
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• pp.829-837
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• 1995

This study was performed to evaluate the effects of ocular bacteria and tear lactoferrin on the Tear Staining Syndrome(TSS) in poodle dogs. Staphylococcus, Klebsiella, Micrococcus and Pseudomonas were the most Prevalent microorganisms isolated in normal eyes of poodle dogs, whereas the predominant isolates in the poodle dogs with TSS were Micrococcus, Staptococcus and Staphylococcus. There were no significant differences between the normal and tear-stained poodle dogs in the quantity of tear lactoferrin. In vitro hair staining experiment, bacteria isolated from the eyes with TSS and lactoferrin didn't stain hair. The results have shown that either ocular bacteria or tear lactoferrins were not related to the TSS.

• ALGAE
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• v.28 no.4
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• pp.379-387
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• 2013

The purpose of this study was to express bovine lactoferrin N-lobe in Chlorella vulgaris, a green microalga, using the pCAMBIA1304 vector. Chlorella-codon-optimized bovine lactoferrin N-lobe (Lfb-N gene) was cloned in the expression vector pCAMBIA1304, creating the plasmid pCAMLfb-N. pCAMLfb-N was then introduced into C. vulgaris by electro-transformation. Transformants were separated from BG-11 plates containing 20 ${\mu}g\;mL^{-1}$ hygromycin. Polymerase chain reaction was used to screen transformants harboring Lfb-N gene. Finally, total soluble protein was extracted from the transformants, and the expression of Lfb-N protein was detected using western blotting. Using this method, we successfully expressed bovine lactoferrin in C. vulgaris. Therefore, our results suggested that recombinant lactoferrin N-lobe, which has many uses in the biomedical and pharmaceutical industries, can be produced economically.

• Journal of Microbiology and Biotechnology
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• v.27 no.10
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• pp.1877-1884
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• 2017

Mesenchymal stem cells (MSCs) have been suggested as a primary candidate for cell therapy applications because they have self-renewal and differentiation capabilities. Although they can be expanded in ex vivo system, clinical application of these cells is still limited because they survive poorly and undergo senescence or apoptosis when transplanted and exposed to environmental factors such as oxidative stress. Thus, reducing oxidative stress is expected to improve the efficacy of MSC therapy. The milk protein lactoferrin is a multifunctional iron-binding glycoprotein that plays various roles, including reduction of oxidative stress. Thus, we explored the effect of lactoferrin on oxidative stress-induced senescence and apoptosis of human MSCs (hMSCs). Measurement of reactive oxygen species (ROS) revealed that lactoferrin inhibited the production of hydrogen peroxide-induced intracellular ROS, suggesting lactoferrin as a good candidate as an antioxidant in hMSCs. Pretreatment of lactoferrin suppressed hydrogen peroxide-induced senescence of hMSCs. In addition, lactoferrin reduced hydrogen peroxide-induced apoptosis via inhibition of caspase-3 and Akt activation. These results demonstrate that lactoferrin can be a promising factor to protect hMSCs from oxidative stress-induced senescence and apoptosis, thus increasing the efficacy of MSC therapy.