Reaction kinetics of pressure-induced denaturation of bovine immunoglobulin G

Mazri, Chafiaa; Ramos, Sergio José; Sánchez, Lourdes; Calvo, Miguel; Pérez, María D.

doi:10.1016/j.idairyj.2011.12.003

Cited by 7 publications

(5 citation statements)

References 21 publications

(33 reference statements)

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“…Unfolded β-LG can form disulfide-bonded aggregates with κ-CN via thioldisulfide bond exchange (Baier et al, 2015a;Bravo et al, 2013Bravo et al, , 2012. These exchanges resulted in greater denaturation of β-LG and α-LA in milk than in whey or buffer, potentially due to the smaller number of molecules available for interaction or aggregation, owing mainly to the absence of CN in whey (Huppertz et al, 2019;Mazri, Ramos, et al, 2012;Patel & Huppertz, 2014). Interestingly, adding sulfhydryl-blocking agents inhibited the association between β-LG and CNs by preventing disulfide bond formation, thus avoiding the aggregation of β-LG (Bravo et al, 2012).…”

Section: 21mentioning

confidence: 99%

“…As a result, β‐LG can form aggregates with WPs via SS–SH exchange. Due to the presence of β‐LG in milk and whey, denaturation of WPs in the latter was reported at higher pressure levels than in buffer (Franco et al., 2018; Mayayo et al., 2014; Mazri, Ramos, et al., 2012; Mazri et al., 2012a). Interestingly, LF in bovine milk was found to have higher sensitivity than in human milk, owing mainly to the lack of β‐LG in human milk.…”

Section: Effect Of Hhp On the Modification Of Wpsmentioning

confidence: 99%

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Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Gharbi

Marciniak

Doyen

2022

Comp Rev Food Sci Food Safe

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High hydrostatic pressure (HHP) treatment induces structural changes in bovine milk proteins depending on factors such as the temperature, pH, concentration, decompression rate, cycling, composition of the medium and pressure level and duration. An in-depth understanding of the impact of these factors is important for controlling HHP-induced modification of milk proteins and the interactions within or between them, which can be applied to prevent undesired aggregation, gelation, and precipitation during HHP processing or to obtain specific milk protein modifications to attain specific protein properties. In this regard, understanding the influences of these factors can provide insight into the modulation and optimization of HHP conditions to attain specific milk protein structures. In recent years, there has been a great research attention on HHP-induced changes in milk proteins influenced by factors such as pH, temperature, concentration, cycling, decompression condition, and medium composition. Hence, to provide insight into how these factors control milk protein structures under HHP treatment and to understand if their effects depend on HHP parameters and environmental conditions, this review discusses recent findings on how various factors (pH, temperature, cycling, decompression rate, medium composition, and concentration) affect HHP-induced bovine milk protein modification. K E Y W O R D Sbovine milk proteins, high hydrostatic pressure, structural changes Practical Application: The information provided in this review will be very useful to anticipate the challenges related to the formulation and development of pressure-treated milk and dairy products.

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Section: 21mentioning

confidence: 99%

Section: Effect Of Hhp On the Modification Of Wpsmentioning

confidence: 99%

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Gharbi

Marciniak

Doyen

2022

Comp Rev Food Sci Food Safe

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“…The concentration of IgG, b-lactoglobulin and a-lactalbumin was measured by radial immunodifusion according to Mazri, Ramos, S anchez, Calvo, & P erez, 2012;Mazri, S anchez, Ramos, Calvo, & P erez, 2012a. Lactoferrin was quantified using a sandwich ELISA and enzymatic activity of lactoperoxidase was measured by a spectrophotometric technique (Mazri, S anchez, Ramos, Calvo, & P erez, 2012b).…”

Section: Determination Of Protein Concentration and Enzymatic Activitymentioning

confidence: 99%

“…Kinetic studies on denaturation of those whey proteins at pressures from 450 to 700 MPa for different holding times have been published (Mazri et al, 2012;Mazri et al, 2012 a, b). In the present work, treatment of milk, whey and buffer at 600 MPa for 15 min has been performed and results did not show significant differences (p < 0.05) with those previously reported.…”

Section: Effect Of High Pressure Treatment On Whey Protein Denaturationmentioning

confidence: 99%

Effect of high pressure treatment on inactivation of vegetative pathogens and on denaturation of whey proteins in different media

Ramos

Chiquirrín

García

et al. 2015

LWT - Food Science and Technology

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“…The effect of high pressure on some milk proteins has been previously investigated in our group. 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).…”

mentioning

confidence: 99%

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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Reaction kinetics of pressure-induced denaturation of bovine immunoglobulin G

Cited by 7 publications

References 21 publications

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review

Effect of high pressure treatment on inactivation of vegetative pathogens and on denaturation of whey proteins in different media

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

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