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

Tabilo‐Munizaga, Gipsy; Gordon, Trudy Ann; Villalobos‐Carvajal, Ricardo; Moreno‐Osorio, Luis; Salazar, Fernando N.; Pérez‐Won, Mario; Acuña, Sergio

doi:10.1016/j.foodchem.2014.01.051

Cited by 60 publications

(35 citation statements)

References 39 publications

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“…To highlight the evolution of the secondary structure on fish proteins based on the time after HHP treatment, the height of the peak of the second derivatives was used for the bands located at 1,609-1,628 cm -1 (intermolecular aggregated b-sheet), 1,628-1,639 cm -1 (intramolecular aggregated b-sheet), 1,639-1,653 cm -1 (a-helix), and 1,653-1,667 cm -1 (turn structures) [41]. Figure 2 shows the effect of the HHP treatment (450 and 550 MPa for 3 and 4 min) on the secondary structure of palm ruff muscle proteins in the prerigor (Fig.…”

Section: Resultsmentioning

confidence: 99%

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

et al. 2015

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The aim of this study was to evaluate the effect of HHP and rigor state on palm ruff (Seriolella violacea) muscle proteins. HHP treatments were performed at 450-550 MPa for 3 and 4 min at 15°C. Protein secondary structure was evaluated by using Fourier transform infrared spectroscopy, and the thermal behavior was evaluated by using differential scanning calorimetry. The results showed that HHP treatments reduced a-helix and increased b-sheet in fish protein structures. Throughout the 35-d storage period, secondary structures in HHP samples changed depending on pressure intensity, holding time, and rigor state. The thermograms of palm ruff muscles showed four endothermic transitions in prerigor state and three in postrigor state. The HHP treatment affected thermal stability of myosin protein, which is reflected in the change of denaturation temperature (T d ) and a decrease in denaturation enthalpy (DH d ) with respect to the native protein; actin was denatured by the pressure treatments. In conclusion, rigor state and HHP affected protein structure of fish proteins.

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Section: Resultsmentioning

confidence: 99%

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

et al. 2015

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“…High pressure (over 100 MPa) is utilized in the food industry for sterilization and preserving flavor and color [1,[5][6][7][8]. It is also used in enzymatic catalysis, since it can stabilize or increase enzyme activities in different operational conditions [9].…”

Section: Introductionmentioning

confidence: 99%

Stability and activity of Dictyoglomus thermophilum GH11 xylanase and its disulphide mutant at high pressure and temperature

Voutilainen

Ojamo

et al. 2015

Enzyme and Microbial Technology

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“…The common cause of these changes is the activation or inactivation of biological enzymes (22). An enzyme is a type of protein, and the impact of high-pressure processing on its structure is shown by several aspects, for example, an unchanged primary structure with unfolding and disassociation of the secondary, tertiary, and quaternary structures (23), the exposure of interior hydrophobic and sulfhydryl groups (24), and the denaturation, aggregation, and gelation of protein molecules, as well as changes to their interfacial properties (25). On the other hand, a change in chemical composition will be reflected in an increase/decrease of flavor or color substances.…”

Section: Zusammenfassungmentioning

confidence: 99%

Effect and Mechanism of High-Pressure Processing: A Case Study of Flue-Cured Tobacco

Tan

Yang

et al. 2017

Beiträge Zur Tabakforschung International/Contributions to Tobacco Research

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Summary After a high-pressure processing (HPP) treatment sensory evaluation of flue-cured tobacco showed modifications. There was no significant difference (P > 0.05) between the routine chemical components (total sugar, reducing sugar, nicotine, and total nitrogen) of flue-cured tobacco after high-pressure processing treatment (HPP sample) and that of an untreated control group (CG). An overall judgement, which can be made from the observations of scanning electron microscopy (SEM), X-ray computed microtomography (micro-CT) and transmission electron microscopy (TEM), is that HPP could compress the inner tunnel and tissue gap in a flue-cured tobacco leaf. However, the ultrastructure, such as the cellular cytoskeleton, would not be changed. Compared with CG, the apparent density of the HPP sample rose by 19.3%, while the true density only rose by 1.4%. This also explained that the main effect of high-pressure processing on flue-cured tobacco was microstructure compression rather than compression on the ultrastructure level. The differences between the lamina (leaf-shaped) sample, which were caused by high-pressure processing, were reflected in terahertz time-domain spectroscopy (THz-TDS), simultaneous thermal analysis (STA), and pyrolysis gas chromatography/mass spectrometry (Py-GC/MS). When the same tests were carried out using a sample that was milled to a powder, however, these differences were nearly removed. The milling process destroyed most of the microstructure of the flue-cured tobacco lamina; therefore, the results of THz-TDS, STA, and Py-GC/MS confirmed the hypothesis: That 400 MPa high-pressure processing treatment minimally changes the ultrastructure of flue-cured tobacco and only changes its relatively larger microstructure.

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

Cited by 60 publications

References 39 publications

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

Protein Changes Caused by High Hydrostatic Pressure (HHP): A Study Using Differential Scanning Calorimetry (DSC) and Fourier Transform Infrared (FTIR) Spectroscopy

Stability and activity of Dictyoglomus thermophilum GH11 xylanase and its disulphide mutant at high pressure and temperature

Effect and Mechanism of High-Pressure Processing: A Case Study of Flue-Cured Tobacco

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