A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

Sreedhara, Ashoka; Flengsrud, Ragnar; Prakash, V.; Krowarsch, Daniel; Langsrud, Thor; Kaul, P.; Devold, Tove Gulbrandsen; Vegarud, Gerd Elisabeth

doi:10.1016/j.idairyj.2010.02.003

Cited by 66 publications

(51 citation statements)

References 49 publications

(53 reference statements)

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“…It was also observed that, IgG and LF in liquid whey were less denatured when heated at lower pH which is far away from pI, this phenomena is in agreement with other studies in pure whey proteins (Dissanayake, Ramchandran, Piyadasa et al 2013). In general, at low pH, strong hydrogen bonds forms protein networks which inhibits activation of thiol group and monomer repulsive electrostatic interactions during unfolding and aggregation processes (Sreedhara et al 2010). According to Wakabayashi et al (2006) reported heat stability of bovine LF in acidic conditions with minimal aggregation in solutions for 5 min at 80 to 120 o C compared to neutral pH.…”

Section: Effect Of Heat On Igg and Lf Concentration In Liquid Whey Wisupporting

confidence: 89%

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

Shimo

Ding

et al. 2016

AJDFR

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The aim of this study was to characterize the effect of heat denaturation on Immunoglobulin G (IgG) and Lactoferrin (LF) in yak milk and colostral liquid whey at medium acidic conditions in presence of protectants (CaCl 2 ; Glycerol and Sodium Dodecyl Sulphate -SDS). Results indicated significant (P < 0.05) heat stability improvement of IgG and LF in liquid whey samples at medium acidic and temperature (72 -90 o C) with less precipitates formation regardless of type of protectants added especially at pH 3.5 and 4.6. The mean concentration values for IgG percentage reduction (72 -90 o C; pH 3.5 -5.5; protectants) ranged from 6 to 26% and 15 to 31% in yak milk and colostral liquid whey, respectively. The percentage of heat denaturation effect for LF ranged from 11 to 32% and 14 to 38% in yak milk and colostral liquid whey, respectively. Application of glycerol in both environmental processing conditions was the most effective in heat stability improvement followed by SDS and CaCl 2 .

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Section: Effect Of Heat On Igg and Lf Concentration In Liquid Whey Wisupporting

confidence: 89%

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

Shimo

Ding

et al. 2016

AJDFR

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“…42) It is accepted that calorimetry and tryptophan fluorescence reflect changes in the conformation of proteins, but do not measure precisely the same parameters. When a protein treated at high pressure is subjected to DSC, the heat flow breaks the bonds that maintain its structure, causing denaturation and in some cases aggregation, but the intensity of fluorescence reveals the movement of tryptophan residues from the inner part of the protein to the surface.…”

Section: Discussionmentioning

confidence: 99%

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

Franco

Castillo

Pérez

et al. 2012

Bioscience, Biotechnology, and Biochemistry

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“…Caprine LF was purified ([95%) using the cation exchange membrane chromatography method (Sreedhara et al 2010).…”

Section: Preparation Of Apo and Holo Forms Of Caprine And Bovine Lactmentioning

confidence: 99%

“…The thermal denaturation of human LF in relation to Fe binding was studied by differential scanning calorimetry (Mata et al 1998;Conesa et al 2007). In a previous study (Sreedhara et al 2010), a comparison between cLF and bLF was done with regard to the conformation and thermal stability. The native cLF showed a lower thermal stability than bLF.…”

Section: Introductionmentioning

confidence: 99%

Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

et al. 2010

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Apo and holo forms of lactoferrin (LF) from caprine and bovine species have been characterized and compared with regard to the structural stability determined by thermal denaturation temperature values (T (m)), at pH 2.0-8.0. The bovine lactoferrin (bLF) showed highest thermal stability with a T (m) of 90 ± 1°C at pH 7.0 whereas caprine lactoferrin (cLF) showed a lower T (m) value 68 ± 1°C. The holo form was much more stable than the apo form for the bLF as compared to cLF. When pH was gradually reduced to 3.0, the T (m) values of both holo bLF and holo cLF were reduced showing T (m) values of 49 ± 1 and 40 ± 1°C, respectively. Both apo and holo forms of cLF and bLF were found to be most stable at pH 7.0. A significant loss in the iron content of both holo and apo forms of the cLF and bLF was observed when pH was decreased from 7.0 to 2.0. At the same time a gradual unfolding of the apo and holo forms of both cLF and bLF was shown by maximum exposure of hydrophobic regions at pH 3.0. This was supported with a loss in α-helix structure together with an increase in the content of unordered (aperiodic) structure, while β structure seemed unchanged at all pH values. Since LF is used today as fortifier in many products, like infant formulas and exerts many biological functions in human, the structural changes, iron binding and release affected by pH and thermal denaturation temperature are important factors to be clarified for more than the bovine species.

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A comparison of effects of pH on the thermal stability and conformation of caprine and bovine lactoferrin

Cited by 66 publications

References 49 publications

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

Heat stability improvement of antimicrobial whey proteins fromyak milk and colostrum at various acidic conditions

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

Structural characteristic, pH and thermal stabilities of apo and holo forms of caprine and bovine lactoferrins

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