Pressure effects on protein secondary structure and hydrogen deuterium exchange in chymotrypsinogen: a Fourier transform infrared spectroscopic study

Pressure‐Tuning the Conformation of Bovine Pancreatic Trypsin Inhibitor Studied by Fourier‐Transform Infrared Spectroscopy

“…We observe pressure-induced changes in the amide I' region (1600-1700 c n -' ) of the spectrum. The features of the secondary structure remain distinct up to 1.5 GPa, in contrast to most proteins where the spectrum becomes featureless at 1 GPa due to denaturation (Wong and Heremans, 1988;Wong, 1991;Takeda et al, 1995). Our experiments suggest that the process is reversible.…”

“…In the plastic regime we expect two possibilities : the change in conformation may be reversible or irreversible. Absorption and fluorescence studies of pressure-induced denaturation in proteins have shown reversible changes in many cases (Weber and Drickamer, 1983) whereas Raman spectroscopy studies for lysozyme (Heremans and Wong, 1985) and FTIR studies for chymotrypsinogen (Wong and Heremans, 1988 ;Wong, 1991) show irreversible pressure effects. This may be due to the large concentrations used in the latter methods so that the intermolecular interactions become more pronounced.…”

“…Pressure-induced changes in the conformation of proteins can conveniently be detected from the changes in the absorption, fluorescence or NMR spectroscopy (Weber and Drickamer, 1983;Zhang et al, 1995). The effect of temperature and pressure on the sccondary structure can be studied by Fourier-transform infrared (FTIR) spectroscopy (Wong and Heremans, 1988;Wong, 1991 ;Fabian et al, 1993;Smeller et al, 1995a;Takeda et al, 1995).…”

Commercial opportunities and research challenges in the high pressure processing of foods

“…In experiments on lysozyme, it has been shown that the pressure at which denaturation starts is higher when pressure is applied more slowly (Heremans & Wong, 1985;Wong & Heremans, 1988). This is important as it suggests that the dynamic aspects of pressure processing may play an important role in microbial inactivation.…”

Changes in functionality of whey protein and micellar casein after high pressure – low temperature treatments

“…It is generally accepted that changes in the molecular structure like refolding or disulfide exchanges can induce large changes in the functional behavior of proteins. Under high pressure, reactions with a negative reaction volume are favored which provide the opportunity to modify protein structures (Belloque, Lopez-Fandino, & Smith, 2000;Gaucheron et al, 1997;Gekko & Hasegawa, 1989;Gekko & Noguchi, 1979;Heremans & Wong, 1985;Huppertz, Fox, & Kelly, 2004a;Wong & Heremans, 1988) and, thus, their functional properties. Former studies showed that high pressure e low temperature (HPLT) treatments induce different structural changes in milk proteins in comparison to high pressure treatments at room temperature (Baier, Purschke, Rawel, Schmitt, & Knorr, submitted for publication;Gebhardt, Toro-Sierra, & Kulozik, 2012;Kolakowski, Dumay, & Cheftel, 2001).…”