Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Moosavi-Movahedi, Ali Akbar; Rajabzadeh, Halimeh; Amani, Mojtaba; Nourouzian, D; Zare, Karim; Hadi, Hassan; Sharifzadeh, Ahmad; Poursasan, Najmeh; Ahmad, Faizan

doi:10.1016/j.ijbiomac.2011.06.020

Cited by 5 publications

(6 citation statements)

References 48 publications

(57 reference statements)

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“…Whole casein fraction and purified ␤-CN are capable to suppress the thermal and chemical aggregation of several substrate proteins. As reported before, ␤-CN has a higher chaperone-like activity than other caseins most likely because of its amphiphilic nature [26][27][28][29][30].…”

Section: Introductionsupporting

confidence: 54%

A new aspect to chaperone-like activity of bovine β-casein by protein–protein interactions study

Sharifizadeh¹,

Saboury²,

Moosavi-Movahedi³

et al. 2012

International Journal of Biological Macromolecules

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Section: Introductionsupporting

confidence: 54%

A new aspect to chaperone-like activity of bovine β-casein by protein–protein interactions study

Sharifizadeh¹,

Saboury²,

Moosavi-Movahedi³

et al. 2012

International Journal of Biological Macromolecules

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“…Previous studies (Moosavi‐Movahedi et al ., ) have shown that β‐casein binds to hydrophobic patches that are exposed due to protein unfolding under unfavourable conditions, such as elevated temperature. Binding of β‐casein to the hydrophobic patches may prevent a random unfolding and thereby facilitate a refolding upon temperature decrease.…”

Section: Resultsmentioning

confidence: 92%

“…Various effects of b-casein acting as either chaperone or having the opposite effect on proteins were reported in recent years. These included highly efficient chaperone effect [presence of b-casein reduced aggregation and improved activity recovery by carbonic anhydrase (Khodarahmi et al, 2008)] as well as antichaperone properties [high b-casein concentration resulted in blocking of lysozyme refolding upon cooling (Wu et al, 2011) and increased aggregation rate (Moosavi-Movahedi et al, 2011)]. In studies done by Hassanisadi (Hassanisadi et al, 2008), it was shown that b-casein can preferentially bind to the aggregation-prone intermediate of horse alcohol dehydrogenase during heat treatment.…”

Section: Introductionmentioning

confidence: 99%

Chaperone‐like activity of β‐casein and its effect on residual in vitro activity of horseradish peroxidase

Sulewska

Olsen

Sørensen

et al. 2014

Int J of Food Sci Tech

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Summary In this study, the residual activity horseradish peroxidase was used as a novel marker of chaperone‐like activity of β‐casein under elevated temperature. It was shown that β‐casein does affect residual activity of horseradish peroxidase (HRP) depending on the concentration and molar ratio between proteins. Incubating HRP (0.1 mg mL−1) for 10 min at 72 °C resulted in residual activity of 59 ± 5%, while addition of 1 mg mL−1 β‐casein resulted in increase in residual activity up to 85 ± 1%. Increased residual activity is not merely attributed to an effect of higher total protein concentration, as similar experiment with bovine serum albumin resulted in residual activity of horseradish peroxidase that was significantly lower than without any addition. The effect of β‐casein on HRP disappears when pH is below the isoelectric point of β‐casein. It was also proven by light scattering studies that β‐casein interacts with horseradish peroxidase when the temperature was increased from 25 to 70 °C whereas interactions seem to cease when temperature was lowered back to 25 °C. This study highlights how specific proteins can influence enzyme activity, which is of potential importance for various industries such as enzyme manufacturers and food industry.

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“…Previous studies have already addressed the effects of the association of HEWL and bovine caseins on the structure of lysozyme. , The association of HEWL and bovine sodium caseinate or micellar casein can lead to a decrease in secondary structure elements in the lysozyme, mainly α-helical structure, but not to a change in the tertiary structure . The association of lysozyme and β-casein also appears to destabilize the lysozyme indicated through a lower melting point and enthalpy measured with differential scanning calorimetry . Nevertheless, de Roos et al showed that the association of hen egg white lysozyme with nonmicellar bovine caseins has no effect on the in vitro enzymatic activity against cell walls of M.…”

Section: Resultsmentioning

confidence: 99%

Natural Association of Lysozyme and Casein Micelles in Human Milk

Jaeser

Moeckel

Weigel

et al. 2022

J. Agric. Food Chem.

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Using reversed phase high-performance liquid chromatography with ultraviolet (UV) detection and electrospray ionization (ESI)-quadrupole time-of-flight mass spectrometry (RP-HPLC-UV-ESI-Q-TOF), the lysozyme content in the milk of 10 volunteering mothers was quantified, ranging from 29 to 96 μg/mL. Following ultracentifugation, it was found that the lysozyme in human milk, unlike other whey proteins, is mainly bound to casein micelles (ca. 75%). The enzymatic activity of human lysozyme, measured as lytic activity against cell walls of Micrococcus lysodeikticus, was similar for the micelle-bound and free protein, indicating that the micellar structure should not affect the antibacterial activity of lysozyme. The results indicate that lysozyme is an integral component of casein micelles in human milk.

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Acidic residue modifications restore chaperone activity of β-casein interacting with lysozyme

Cited by 5 publications

References 48 publications

A new aspect to chaperone-like activity of bovine β-casein by protein–protein interactions study

A new aspect to chaperone-like activity of bovine β-casein by protein–protein interactions study

Chaperone‐like activity of β‐casein and its effect on residual in vitro activity of horseradish peroxidase

Natural Association of Lysozyme and Casein Micelles in Human Milk

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