Effect of high‐pressure processing on myofibrillar protein structure

Abstract

Modification of myofibrillar proteins induced by high-pressure processing has been investigated at pressures ranging from 50 to 600 MPa for 10 min at 20 • C. Analysis by spectroscopic methods and circular dichroism of myofibrillar proteins in phosphate buffer pH 6.0 containing 0.6 M KCl showed no changes in the secondary structure of proteins. However, study of protein conformation by quasielastic light scattering and gel filtration chromatography proved the emergence of aggregation after treatment at pressures higher than 300 MPa. This aggregation was accompanied by enhanced binding of anilino-1-naphthalene-8-sulphonic acid, which indicated an increase in hydrophobic bonding of myofibrillar proteins. Modification of the tertiary and quaternary structures of proteins may induce a molten globule state.

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

“…2a, b) regardless of the pressure treatment and rigor state. These results agree with those reported by Chapleau et al [11]. High hydrostatic pressure generated changes in the protein secondary structure and affected non-covalent interactions within the protein molecules [4]; however, the bonds or intermolecular and intramolecular interactions can undergo reformation [28], which can generate an increase or preservation of some secondary structure conformations [39,44].…”

“…Structural transitions of proteins under high pressure are often driven by the hydration changes that accompany protein conformational transitions [34]. The most pressure labile protein structures are the quaternary and tertiary structures; major changes are observed beyond 100 MPa [11]. Some parts of the secondary structure, such as the b structures, are preserved and remain unchanged with HHP processing, which depends on time and pressure level as observed by Winter and Dzwolak [44] in staphylococcal nuclease and Zhang et al [47] in ribonuclease A.…”

Physicochemical changes induced in carp (Cyprinus carpio) fillets by high pressure processing at low temperature

“…Studies have also been reported on HP inactivation of enzymes and pathogens in various fruit juices (Bayindirli, Alpas, Bozoglu, & Hizal, 2006), such as HP inactivation of pectinmethylesterase in carrot juice (Balogh, Smout, Nguyen, Van Loey, & Hendrickx, 2004), and HP inactivation of Escherichia coli and Listeria monocytogenes in alfalfa seeds (Ariefdjohan et al, 2004). More recent studies on the pressure effects on food and related systems include those by Chapleau, Mangavel, Campoint, and de Lamballerie-Anton (2003) that verified how pressure influenced beef myofibrillar protein structure. The influence of pressure on the quality of salmon that had been cold-smoked and vacuum packaged during refrigerated storage has also been investigated (Lakshmann, Miskin, & Piggott, 2005).…”

Convective Drying of Osmo-Treated Abalone (Haliotis rufescens) Slices: Diffusion, Modeling, and Quality Features

“…In particular, Vega-Gálvez et al [29] working in cuttlefish found similar results. Besides, it must be pointed out that abalone and all the meat species have a good water holding capacity, due to their protein feature of a myofibril origin [52]. Table 2 show that the antioxidant capacity obtained a decrease with the process temperatures; that is, it can be observed that the variable temperature has a significant effect on the antioxidant activity of the abalone samples.…”

“…The myofibrils proteins such as the myosin play an important role in the quality of meat owing to their capacity to hold water [52].…”