Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics
This study investigated structural changes in β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH h...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-12-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/24/7650 |
| _version_ | 1797502118291046400 |
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| author | Tatijana Markoska Davor Daniloski Todor Vasiljevic Thom Huppertz |
| author_facet | Tatijana Markoska Davor Daniloski Todor Vasiljevic Thom Huppertz |
| author_sort | Tatijana Markoska |
| collection | DOAJ |
| description | This study investigated structural changes in β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH had strongly affected the secondary structure of β-casein, with most affected regions involving random coils and α-helical structures. The α-helical structures showed great pH sensitivity by decreasing at 20 °C and diminishing completely at 4 °C when pH was increased from 5.9 to 7.0. The decrease in α-helix was likely related to the greater presence of random coils at pH 7.0, which was not observed at pH 5.9 at either temperature. The changes in secondary structure components were linked to decreased hydrophobic interactions at lower temperature and increasing pH. The most prominent change of the α-helix took place when the pH was adjusted to 7.0 and the temperature set at 4 °C, which confirms the disruption of the hydrogen bonds and weakening of hydrophobic interactions in the system. The findings can assist in establishing the structural behaviour of the β-casein under conditions that apply as important for solubility and production of β-casein. |
| first_indexed | 2024-03-10T03:28:19Z |
| format | Article |
| id | doaj.art-7212fe6fde184759acafb7a0d6062d40 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T03:28:19Z |
| publishDate | 2021-12-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-7212fe6fde184759acafb7a0d6062d402023-11-23T09:47:16ZengMDPI AGMolecules1420-30492021-12-012624765010.3390/molecules26247650Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and ChemometricsTatijana Markoska0Davor Daniloski1Todor Vasiljevic2Thom Huppertz3Advanced Food Systems Research Unit, Institute for Sustainable Industries & Liveable Cities, College of Health and Biomedicine, Victoria University, Melbourne, VIC 8001, AustraliaAdvanced Food Systems Research Unit, Institute for Sustainable Industries & Liveable Cities, College of Health and Biomedicine, Victoria University, Melbourne, VIC 8001, AustraliaAdvanced Food Systems Research Unit, Institute for Sustainable Industries & Liveable Cities, College of Health and Biomedicine, Victoria University, Melbourne, VIC 8001, AustraliaAdvanced Food Systems Research Unit, Institute for Sustainable Industries & Liveable Cities, College of Health and Biomedicine, Victoria University, Melbourne, VIC 8001, AustraliaThis study investigated structural changes in β-casein as a function of temperature (4 and 20 °C) and pH (5.9 and 7.0). For this purpose, nuclear magnetic resonance (NMR) and Fourier-transform infrared (FTIR) spectroscopy were used, in conjunction with chemometric analysis. Both temperature and pH had strongly affected the secondary structure of β-casein, with most affected regions involving random coils and α-helical structures. The α-helical structures showed great pH sensitivity by decreasing at 20 °C and diminishing completely at 4 °C when pH was increased from 5.9 to 7.0. The decrease in α-helix was likely related to the greater presence of random coils at pH 7.0, which was not observed at pH 5.9 at either temperature. The changes in secondary structure components were linked to decreased hydrophobic interactions at lower temperature and increasing pH. The most prominent change of the α-helix took place when the pH was adjusted to 7.0 and the temperature set at 4 °C, which confirms the disruption of the hydrogen bonds and weakening of hydrophobic interactions in the system. The findings can assist in establishing the structural behaviour of the β-casein under conditions that apply as important for solubility and production of β-casein.https://www.mdpi.com/1420-3049/26/24/7650FTIRNMRβ-caseinsecondary structuretemperaturepH |
| spellingShingle | Tatijana Markoska Davor Daniloski Todor Vasiljevic Thom Huppertz Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics Molecules FTIR NMR β-casein secondary structure temperature pH |
| title | Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics |
| title_full | Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics |
| title_fullStr | Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics |
| title_full_unstemmed | Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics |
| title_short | Structural Changes of β-Casein Induced by Temperature and pH Analysed by Nuclear Magnetic Resonance, Fourier-Transform Infrared Spectroscopy, and Chemometrics |
| title_sort | structural changes of β casein induced by temperature and ph analysed by nuclear magnetic resonance fourier transform infrared spectroscopy and chemometrics |
| topic | FTIR NMR β-casein secondary structure temperature pH |
| url | https://www.mdpi.com/1420-3049/26/24/7650 |
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