TY - JOUR
T1 - Effects of high hydrostatic pressure (HHP) on the protein structure and thermal stability of Sauvignon blanc wine
AU - Tabilo-Munizaga, Gipsy
AU - Gordon, Trudy Ann
AU - Villalobos-Carvajal, Ricardo
AU - Moreno-Osorio, Luis
AU - Salazar, Fernando N.
AU - Pérez-Won, Mario
AU - Acuña, Sergio
N1 - Funding Information:
The authors gratefully acknowledge the financial support from the FONDEF program ( project number D10I1170 ).
PY - 2014/7/15
Y1 - 2014/7/15
N2 - Protein haze development in bottled white wines is attributed to the slow denaturation of unstable proteins, which results in their aggregation and flocculation. These protein fractions can be removed by using bentonite; however, a disadvantage of this technique is its cost. The effects of high hydrostatic pressure (HHP) on wine stability were studied. Fourier transform infrared spectroscopy experiments were performed to analyse the secondary structure of protein, thermal stability was evaluated with differential scanning calorimetry, while a heat test was performed to determine wine protein thermal stability. The results confirmed that high pressure treatments modified the α-helical and β-sheet structures of wine proteins. Throughout the 60 days storage period the α-helix structure in HHP samples decreased. Structural changes by HHP (450 MPa for 3 and 5 min) improve thermal stability of wine proteins and thus delay haze formation in wine during storage.
AB - Protein haze development in bottled white wines is attributed to the slow denaturation of unstable proteins, which results in their aggregation and flocculation. These protein fractions can be removed by using bentonite; however, a disadvantage of this technique is its cost. The effects of high hydrostatic pressure (HHP) on wine stability were studied. Fourier transform infrared spectroscopy experiments were performed to analyse the secondary structure of protein, thermal stability was evaluated with differential scanning calorimetry, while a heat test was performed to determine wine protein thermal stability. The results confirmed that high pressure treatments modified the α-helical and β-sheet structures of wine proteins. Throughout the 60 days storage period the α-helix structure in HHP samples decreased. Structural changes by HHP (450 MPa for 3 and 5 min) improve thermal stability of wine proteins and thus delay haze formation in wine during storage.
KW - Haze formation
KW - High hydrostatic pressure
KW - Melting temperature
KW - Pathogenesis-related (PR) proteins
KW - Secondary structure of protein
KW - Wine protein stability
UR - http://www.scopus.com/inward/record.url?scp=84893922261&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2014.01.051
DO - 10.1016/j.foodchem.2014.01.051
M3 - Article
C2 - 24594177
AN - SCOPUS:84893922261
SN - 0308-8146
VL - 155
SP - 214
EP - 220
JO - Food Chemistry
JF - Food Chemistry
ER -