Effects of high hydrostatic pressure (HHP) on protein structure and digestibility of red abalone (Haliotis rufescens) muscle

2020 ◽  
Vol 60 ◽  
pp. 102282 ◽  
Author(s):  
Yamira Cepero-Betancourt ◽  
Mauricio Opazo-Navarrete ◽  
Anja E.M. Janssen ◽  
Gipsy Tabilo-Munizaga ◽  
Mario Pérez-Won
Keyword(s):  
Protein Structure ◽  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Haliotis Rufescens ◽  
Red Abalone

Effects of high hydrostatic pressure (HHP) on the protein structure and thermal stability of Sauvignon blanc wine

2014 ◽  
Vol 155 ◽  
pp. 214-220 ◽  
Author(s):  
Gipsy Tabilo-Munizaga ◽  
Trudy Ann Gordon ◽  
Ricardo Villalobos-Carvajal ◽  
Luis Moreno-Osorio ◽  
Fernando N. Salazar ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Protein Structure ◽  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Sauvignon Blanc ◽  
Thermal Stability Of

scholarly journals Lessons from pressure denaturation of proteins

2018 ◽  
Vol 15 (147) ◽  
pp. 20180244 ◽  
Author(s):  
Julien Roche ◽  
Catherine A. Royer
Keyword(s):  
Protein Structure ◽  
Hydrostatic Pressure ◽  
Protein Stability ◽  
Thermodynamic Parameter ◽  
High Hydrostatic Pressure ◽  
Pressure Effects ◽  
Structure And Stability ◽  
Denaturation Of Proteins

Although it is now relatively well understood how sequence defines and impacts global protein stability in specific structural contexts, the question of how sequence modulates the configurational landscape of proteins remains to be defined. Protein configurational equilibria are generally characterized by using various chemical denaturants or by changing temperature or pH. Another thermodynamic parameter which is less often used in such studies is high hydrostatic pressure. This review discusses the basis for pressure effects on protein structure and stability, and describes how the unique mechanisms of pressure-induced unfolding can provide unique insights into protein conformational landscapes.

Survival of mouse blastocysts after low-temperature preservation under high pressure

2004 ◽  
Vol 52 (4) ◽  
pp. 479-487 ◽  
Author(s):  
Cs. Pribenszky ◽  
M. Molnár ◽  
S. Cseh ◽  
L. Solti
Keyword(s):  
Phase Transition ◽  
Hydrostatic Pressure ◽  
Low Temperature ◽  
High Hydrostatic Pressure ◽  
Room Temperature ◽  
Freezing Point ◽  
Significant Loss ◽  
Embryo Cryopreservation ◽  
Subzero Temperatures ◽  
Survival Capacity

Cryoinjuries are almost inevitable during the freezing of embryos. The present study examines the possibility of using high hydrostatic pressure to reduce substantially the freezing point of the embryo-holding solution, in order to preserve embryos at subzero temperatures, thus avoiding all the disadvantages of freezing. The pressure of 210 MPa lowers the phase transition temperature of water to -21°C. According to the results of this study, embryos can survive in high hydrostatic pressure environment at room temperature; the time embryos spend under pressure without significant loss in their survival could be lengthened by gradual decompression. Pressurisation at 0°C significantly reduced the survival capacity of the embryos; gradual decompression had no beneficial effect on survival at that stage. Based on the findings, the use of the phenomena is not applicable in this form, since pressure and low temperature together proved to be lethal to the embryos in these experiments. The application of hydrostatic pressure in embryo cryopreservation requires more detailed research, although the experience gained in this study can be applied usefully in different circumstances.

Effect of High Hydrostatic Pressure on Endothelial Lipase Expression*

2010 ◽  
Vol 37 (6) ◽  
pp. 641-645 ◽  
Author(s):  
Can-Xin XU ◽  
Chun WANG ◽  
Bing-Yang ZHU ◽  
Zhi-Ping GAO ◽  
Di-Xian LUO ◽  
...  
Keyword(s):  
Hydrostatic Pressure ◽  
High Hydrostatic Pressure ◽  
Endothelial Lipase ◽  
Lipase Expression
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