Effects of ultra‐high pressure on the biochemical properties and secondary structure of myofibrillar protein from Oratosquilla oratoria muscle

Abstract

Oratosquilla oratoria (O. oratoria) were treated with 300, 350, and 400 MPa for 5, 8, and 10 min, respectively. The myofibrillar protein (MP) content, sulfhydryl content, Ca2+‐ATPase activity, surface hydrophobicity and secondary structure of MP were determined to investigate the effects of ultra‐high pressure (UHP) on the biochemical properties and secondary structure of MP from O. oratoria muscle. Results showed that the relatively low pressures have no significant effects on the MP content. When the pressure and holding time increased, the MP content decreased significantly. However, when the pressure condition reached 400 MPa for 10 min, the relative sulfhydryl content and Ca2+‐ATPase activity reduced to 62.76 and 47.88%, respectively, while the relative surface hydrophobicity increased to 132.20%. Moreover, as pressure increased, the β‐Turn and α‐Helix gradually converted to β‐Sheet and Random coil of MP. In short, the biochemical properties and secondary structure of MP from O. oratoria had significant correlations and they interacted with each other. These findings can provide a reference for using UHP to assist the shelling of O. oratoria. Practical applications UHP is an emerging food processing technology that is widely used in the processing of aquatic products, such as shelling. While whether the choice of conditions will affect the meat quality of shelled aquatic products is still less studied. The purpose of this study was to investigate the effects of different UHP parameters on the biochemical characteristics and structure of myofibrillar protein in O. oratoria, and to determine the effects on the quality of O. oratoria meat. These results could provide theoretical guidance for determining the more suitable parameters of UHP, which was conducive to the development of O. oratoria products and the application of UHP technology in aquatic products processing.

Insights into peptide profiling of sturgeon myofibrillar proteins with low temperature vacuum heating

“…At the same time, in addition to the influence of heat, the influence of pressure changes on proteins cannot be ignored. The increase in pressure made the β ‐sheet continuously increase and the α ‐helix decrease ( P < 0.05), which was consistent with the research by Li et al 15 . An increase in pressure caused the hydrogen bond to change, and part of the α ‐helix was thus opened, resulting in a decrease in the content 15 .…”

Effects of High-Pressure Treatments (Ultra-High Hydrostatic Pressure and High-Pressure Homogenization) on Bighead Carp (Aristichthys nobilis) Myofibrillar Protein Native State and Its Hydrolysate

“…The impact of all the treatments on the β-turn content was not signi cant (p > 0.05). The destruction of the α-helix was due to the hydrogen bond change, whereas the signi cant increase in β-sheet content (p < 0.05) and a decrease in random coil might be due to the decrease in particle size (Gaoshang et al 2019). Similar results have been reported that UHP treatment reduced the αhelix content in myo brillar protein from Oratosquilla oratoria muscle (Gaoshang et al 2019) and increased β-sheet content in the myo brillar protein from Trichiurus Haumela Surimi (Chen et al 2020b).…”

“…The destruction of the α-helix was due to the hydrogen bond change, whereas the signi cant increase in β-sheet content (p < 0.05) and a decrease in random coil might be due to the decrease in particle size (Gaoshang et al 2019). Similar results have been reported that UHP treatment reduced the αhelix content in myo brillar protein from Oratosquilla oratoria muscle (Gaoshang et al 2019) and increased β-sheet content in the myo brillar protein from Trichiurus Haumela Surimi (Chen et al 2020b). Shi et al ( 2019) have found the β-turn proportion in the clam shell myo brillar was decreased after HPH treatment, which was inconsistent with our results.…”

“…Considering the advantages of non-thermal physical processing, UHP and HPH have been applied to the processing of different raw materials (Leite As an processing technology, UHP can make the protein structure looser, more cleavage sites exposed by changing non-covalent bonds such as hydrogen bonds and ionic bonds (Ulug et al 2021). Meanwhile, UHP is susceptible to induce protein aggregation via disul de bonds (Gaoshang et al 2019). Therefore, the susceptibility of protein to enzyme was changed.…”

Emulsification through oil addition on the properties of yellowfin tuna ( Thunnus albacares ) paste

“…The amide I region (1,700-1,600 cm −1 ) produced by C = O expansion vibration exhibits a wider peak , and the maximum absorption wavelength was at ~1,656 cm −1 . The amide I band, as the most sensitive indicator of protein secondary structural composition (Kong & Yu, 2007), is a complex mixture of several overlapping protein structural forms (Barth, 2007), where regions 1,640-1,600, 1,650-1,641, 1,660-1,651 and 1,700-1,661 cm −1 represent the β-sheet, random coil, α-helix, and β-turn conformation respectively (Gaoshang et al, 2019). Multi-peak fitting with Gaussian functions was applied using PeakFit 4.11 to quantify the multicomponent peaks in the amide I band (Figure S1).…”