Chaperone-like activity of β-casein and its effect on residual in vitro activity of horseradish peroxidase
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Chaperone-like activity of β-casein and its effect on residual in vitro activity of horseradish peroxidase. / Sulewska, Anna Maria; Olsen, Karsten; Sørensen, Jens Christian; Øgendal, Lars Holm.
In: International Journal of Food Science and Technology, Vol. 49, No. 12, 2014, p. 2538-2545.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Chaperone-like activity of β-casein and its effect on residual in vitro activity of horseradish peroxidase
AU - Sulewska, Anna Maria
AU - Olsen, Karsten
AU - Sørensen, Jens Christian
AU - Øgendal, Lars Holm
PY - 2014
Y1 - 2014
N2 - 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.
AB - 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.
KW - Casein
KW - Enzyme activity
KW - Enzymes
KW - Milk proteins
U2 - 10.1111/ijfs.12600
DO - 10.1111/ijfs.12600
M3 - Journal article
VL - 49
SP - 2538
EP - 2545
JO - International Journal of Food Science and Technology
JF - International Journal of Food Science and Technology
SN - 0950-5423
IS - 12
ER -
ID: 125387036