Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin

This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic pat...
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Autor*in:	Xinhui Zhou [verfasserIn] Cuina Wang [verfasserIn] Xiaomeng Sun [verfasserIn] Zixuan Zhao [verfasserIn] Mingruo Guo [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2020

Schlagwörter:	goat milk β-lactoglobulin high intensity ultrasound physiochemical property structure

Übergeordnetes Werk:	In: Molecules - MDPI AG, 2003, 25(2020), 16, p 3637
Übergeordnetes Werk:	volume:25 ; year:2020 ; number:16, p 3637

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DOI / URN:	10.3390/molecules25163637

Katalog-ID:	DOAJ038726858

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language	English
source	In Molecules 25(2020), 16, p 3637 volume:25 year:2020 number:16, p 3637
sourceStr	In Molecules 25(2020), 16, p 3637 volume:25 year:2020 number:16, p 3637
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institution	findex.gbv.de
topic_facet	goat milk β-lactoglobulin high intensity ultrasound physiochemical property structure Organic chemistry
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container_title	Molecules
authorswithroles_txt_mv	Xinhui Zhou @@aut@@ Cuina Wang @@aut@@ Xiaomeng Sun @@aut@@ Zixuan Zhao @@aut@@ Mingruo Guo @@aut@@
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callnumber-first	Q - Science
author	Xinhui Zhou
spellingShingle	Xinhui Zhou misc QD241-441 misc goat milk β-lactoglobulin misc high intensity ultrasound misc physiochemical property misc structure misc Organic chemistry Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin
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topic_title	QD241-441 Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin goat milk β-lactoglobulin high intensity ultrasound physiochemical property structure
topic	misc QD241-441 misc goat milk β-lactoglobulin misc high intensity ultrasound misc physiochemical property misc structure misc Organic chemistry
topic_unstemmed	misc QD241-441 misc goat milk β-lactoglobulin misc high intensity ultrasound misc physiochemical property misc structure misc Organic chemistry
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title	Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin
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title_full	Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin
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author_browse	Xinhui Zhou Cuina Wang Xiaomeng Sun Zixuan Zhao Mingruo Guo
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title_sort	effects of high intensity ultrasound on physiochemical and structural properties of goat milk β-lactoglobulin
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title_auth	Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin
abstract	This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.
abstractGer	This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.
abstract_unstemmed	This study aimed to compare the effects of high intensity ultrasound (HIU) applied at various amplitudes (20~40%) and for different durations (1~10 min) on the physiochemical and structural properties of goat milk β-lactoglobulin. No significant change was observed in the protein electrophoretic patterns by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Deconvolution and second derivative of the Fourier transform infrared spectra (FTIR) showed that the percentage of β-sheet of goat milk β-lactoglobulin was significantly decreased while those of α-helix and random coils increased after HIU treatment The surface hydrophobicity index and intrinsic fluorescence intensity of samples was enhanced and increased with increasing HIU amplitude or time. Differential scanning calorimetry (DSC) results exhibited that HIU treatments improved the thermal stability of goat milk β-lactoglobulin. Transmission electron microscopy (TEM) of samples showed that the goat milk β-lactoglobulin microstructure had changed and it contained larger aggregates when compared with the untreated goat milk β-lactoglobulin sample. Data suggested that HIU treatments resulted in secondary and tertiary structural changes of goat milk β-lactoglobulin and improved its thermal stability.
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title_short	Effects of High Intensity Ultrasound on Physiochemical and Structural Properties of Goat Milk β-Lactoglobulin
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