TY - JOUR
T1 - The effect of high pressure microfluidization on the structure and length distribution of whey protein fibrils
AU - Oboroceanu, Daniela
AU - Wang, Lizhe
AU - Kroes-Nijboer, Ardy
AU - Brodkorb, André
AU - Venema, Paul
AU - Magner, Edmond
AU - Auty, Mark A.E.
PY - 2011/10
Y1 - 2011/10
N2 - The effect of high pressure microfluidization on native β-lactoglobulin (β-lg) or whey protein isolate (WPI), both before and after heat-induced protein fibril formation at pH 2.0, was investigated using atomic force microscopy (AFM), shear birefringence, reversed phase-high pressure liquid chromatography, attenuated total reflectance-Fourier transform infrared spectroscopy and fluorescence spectroscopy. The morphology and length distribution of the fibrils were determined using AFM and flow-induced birefringence, respectively. High pressure (≥50 MPa) microfluidization treatment of β-lg induced ∼30% protein denaturation, accompanied by changes in secondary structure. Fibrils formed from high pressure treated β-lg or WPI were similar in length to fibrils formed from non-pressure treated proteins. High pressure (≥50 MPa) microfluidization of fibrils formed from β-lg or WPI resulted in their breakup into more uniformly sized and much shorter fibrils. Microfluidization pressures of up to 170 MPa resulted in slightly shorter fibrils but did not completely dissociate them.
AB - The effect of high pressure microfluidization on native β-lactoglobulin (β-lg) or whey protein isolate (WPI), both before and after heat-induced protein fibril formation at pH 2.0, was investigated using atomic force microscopy (AFM), shear birefringence, reversed phase-high pressure liquid chromatography, attenuated total reflectance-Fourier transform infrared spectroscopy and fluorescence spectroscopy. The morphology and length distribution of the fibrils were determined using AFM and flow-induced birefringence, respectively. High pressure (≥50 MPa) microfluidization treatment of β-lg induced ∼30% protein denaturation, accompanied by changes in secondary structure. Fibrils formed from high pressure treated β-lg or WPI were similar in length to fibrils formed from non-pressure treated proteins. High pressure (≥50 MPa) microfluidization of fibrils formed from β-lg or WPI resulted in their breakup into more uniformly sized and much shorter fibrils. Microfluidization pressures of up to 170 MPa resulted in slightly shorter fibrils but did not completely dissociate them.
UR - http://www.scopus.com/inward/record.url?scp=79960359611&partnerID=8YFLogxK
U2 - 10.1016/j.idairyj.2011.03.015
DO - 10.1016/j.idairyj.2011.03.015
M3 - Article
AN - SCOPUS:79960359611
SN - 0958-6946
VL - 21
SP - 823
EP - 830
JO - International Dairy Journal
JF - International Dairy Journal
IS - 10
ER -