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FUNCTIONAL PROPERTIES OF HIGH HYDROSTATIC PRESSURE‐TREATED WHEY PROTEIN
Author(s) -
LEE W.,
CLARK S.,
SWANSON B.G.
Publication year - 2006
Publication title -
journal of food processing and preservation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.511
H-Index - 48
eISSN - 1745-4549
pISSN - 0145-8892
DOI - 10.1111/j.1745-4549.2005.00081.x
Subject(s) - whey protein , chemistry , solubility , hydrostatic pressure , whey protein isolate , emulsion , salt (chemistry) , phosphate , chromatography , phosphate buffered saline , food science , pea protein , biochemistry , organic chemistry , physics , thermodynamics
Surface hydrophobicity, solubility, gelation and emulsifying properties of high hydrostatic pressure (HHP)‐treated whey protein were evaluated. HHP treatment of whey protein buffer or salt solutions were performed at 690 MPa and initial ambient temperature for 5, 10, 20 or 30 min. Untreated whey protein was used as a control. The surface hydrophobicity of whey protein in 0.1 M phosphate buffers treated at pH 7.0 increased with an increase in HHP treatment time from 10 to 30 min. HHP treatments of whey protein in salt solutions at pH 7.0 for 5, 10, 20 or 30 min decreased the solubility of whey proteins. A significant correlation was observed between the surface hydrophobicity and solubility of untreated and HHP‐treated whey protein with r = −0.946. Hardness of HHP‐induced 20, 25 or 30% whey protein gels increased with an increase in HHP treatment time from 5 to 30 min. An increase in the hardness of whey protein gels was observed as whey protein concentration increased. Whey proteins treated in phosphate buffer at pH 5.8 and 690 MPa for 5 min exhibited increased emulsifying activity. Whey proteins treated in phosphate buffer at pH 7.0 and 690 MPa for 10, 20 or 30 min exhibited decreased emulsifying activity. HHP‐treated whey proteins in phosphate buffer at pH 5.8 or 7.0 contributed to an increase in emulsion stability of model oil‐in‐water emulsions. This study demonstrates that HHP treatment of whey protein in phosphate buffer or salt solutions leads to whey protein unfolding observed as increased surface hydrophobicity. Whey proteins treated in phosphate buffers at pH 5.8 and 690 MPa for 5 min may potentially be used to enhance emulsion stability in foods such as salad dressings, sausage and processed cheese.