Effects of Hydrostatic High Pressure on the Structure and Antibacterial Activity of Recombinant Human Lactoferrin from Transgenic Rice

Franco, Indira; Castillo, Eduardo; Pérez, María D.; Calvo, Miguel; Sánchez, Lourdes

doi:10.1271/bbb.110433

Cited by 12 publications

(13 citation statements)

References 46 publications

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“…The susceptibility of LFb to high pressure is similar to that found for human recombinant LF from rice, as both proteins maintained the iron-binding capacity only after treatment at 400 MPa (Franco et al 2011). Some authors have also studied the effect of non-thermal treatments such as pulsed electric field processing (Sui et al 2010) and they showed that iron was not released from the protein in a relatively low ionic strength environment.…”

Section: Resultssupporting

confidence: 59%

“…The results obtained for the effect of HHP on LFb can be compared with those we obtained in a similar study on the effect of HHP on recombinant human LF obtained from rice (Franco et al 2011). On the whole, the calorimetric study of pressure treated recombinant human LF showed less changes in the thermal parameters than those found for LFb, though the apo form of the recombinant protein did not give any peak after treatment at 600 MPa.…”

Section: Resultsmentioning

confidence: 74%

“…We have studied the kinetics of denaturation by high pressure of LFb, lactoperoxidase, α-la, β-lg and immunoglobulins (Mazri et al 2012a, b, c). We have also investigated the effect of high pressure on human LF from transgenic rice (Franco et al 2011). In the case of bovine native (LFb-nat), our previous study showed the influence of the composition of medium in the decrease of LF immunoreactivity after high pressure, by determining the kinetic parameters of the denaturation process (Mazri et al 2012a).…”

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confidence: 99%

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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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Section: Resultssupporting

confidence: 59%

Section: Resultsmentioning

confidence: 74%

mentioning

confidence: 99%

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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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“…Thermal treatment is a traditional technique used to preserve a variety of foodstuffs by inactivating spoilage bacteria and foodborne pathogens (Franco, Castillo, Pérez, Calvo, & Sánchez, ). It involves the use of heat to prepare foods at varying levels of temperature depending upon the type of food and the product being prepared.…”

Section: Introductionmentioning

confidence: 99%

“…Lactoferrin is an 80‐kDa multifunctional glycoprotein with high homology among species, and is found in the milk and most mammalian biological secretion (Franco et al, ). The content of lactoferrin in human milk is more than 1.0 g/L, which is roughly a tenfold concentration higher than that in bovine milk (Masson & Heremans, ).…”

Section: Introductionmentioning

confidence: 99%

Effects of thermal treatment on the physicochemical properties and osteogenic activity of lactoferrin

Fan

Shi

et al. 2019

J Food Process Preserv

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Lactoferrin as a key basic protein in bovine milk has attracted extensive attentions due to its multifunctional activities. Thermal treatment has been widely used during processing of dairy products, which might damage the bioactivity of heat‐sensitive proteins. However, there has been little information on effect of heat treatment on the bioactivity of lactoferrin. In this study, the effects of four different thermal treatments (65°C/30 min, 72°C/10 s, 85°C/10 min, and 95°C/10 min) on lactoferrin were examined by sodium dodecyl sulfate–polyacrylamide gel electrophoresis, circular dichroism spectrum, electron microscope, dynamic light scattering, and semiquantitative RT‐PCR. Results revealed that these treatments altered its second structure and surface hydrophobicity. Moreover, the osteogenic activity of lactoferrin decreased by analyzing the effect of different samples on the mitogen‐activated protein kinase mRNA expression. These findings provided theory data for the research and development of lactoferrin as a functional component in food industry. Practical applications As we know, thermal treatment has been widely used during processing of dairy products. Lactoferrin is a key basic protein component in bovine milk and has a variety of biological activities such as osteogenic activity. However, very few studies have focused on the effect of heat treatment on the osteogenic activity of lactoferrin, thereby limiting its applications. The objective of the present study was to investigate the effects of heating on the structure and osteogenic activity of lactoferrin. Results showed that the regular heat‐processing parameters in dairy industry and structural change of lactoferrin led to the loss of its osteogenic activity. These results will provide some theoretical and practical data for the development of lactoferrin as ingredient in functional food industry.

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Effect of Food Processing on the Mineral-Containing Proteins

Chen

Zhang

Zhao

2017

Mineral Containing Proteins

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Effects of Hydrostatic High Pressure on the Structure and Antibacterial Activity of Recombinant Human Lactoferrin from Transgenic Rice

Cited by 12 publications

References 46 publications

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

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

Effects of thermal treatment on the physicochemical properties and osteogenic activity of lactoferrin

Effect of Food Processing on the Mineral-Containing Proteins

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