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

Cepero-Betancourt, Yamira; Opazo-Navarrete, Mauricio; Janssen, A.E.M.; Tabilo‐Munizaga, Gipsy; Pérez‐Won, Mario

doi:10.1016/j.ifset.2019.102282

Cited by 46 publications

(28 citation statements)

References 45 publications

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“…By using available computational methods, detailed pressure-induced changes in protein secondary structure from characteristic shifts in the band frequencies that are recorded via various techniques, such as Fourier-transform infrared spectroscopy (FTIR), Raman spectra and circular dichroism (CD) [27]. The secondary structure of protein includes α-helix, the β-sheet, β-turn, random coil [28]. The α-helix is stabilized by intramolecular hydrogen bonds between the carbonyl oxygen and amino hydrogen of the polypeptide chain and is buried in the interior site of the protein [29].…”

Section: Secondary Structurementioning

confidence: 99%

“…With an increase in pressure, the intramolecular hydrogen bonds would be destroyed, leading to the transformation of α-helix to β-sheet, β-turn, and random coil, thus resulting in an increase of β-sheet content. It has also been found that abalone proteins are predominantly of β-sheet structure [28]. HHP could disrupt the intermolecular β-sheet structure in abalone proteins, which was compensated for by forming new intramolecular β-sheet interactions [28].…”

Section: Secondary Structurementioning

confidence: 99%

“…It has also been found that abalone proteins are predominantly of β-sheet structure [28]. HHP could disrupt the intermolecular β-sheet structure in abalone proteins, which was compensated for by forming new intramolecular β-sheet interactions [28]. Chen et al found that the β-turn was reduced with the treatment of pressure [37].…”

Section: Secondary Structurementioning

confidence: 99%

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Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Liu

et al. 2021

Foods

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In meat processing, changes in the myofibrillar protein (MP) structure can affect the quality of meat products. High hydrostatic pressure (HHP) has been widely utilized to change the conformational structure (secondary, tertiary and quaternary structure) of MP so as to improve the quality of meat products. However, a systematic summary of the relationship between the conformational structure (secondary and tertiary structure) changes in MP, gel properties and product quality under HHP is lacking. Hence, this review provides a comprehensive summary of the changes in the conformational structure and gel properties of MP under HHP and discusses the mechanism based on previous studies and recent progress. The relationship between the spatial structure of MP and meat texture under HHP is also explored. Finally, we discuss considerations regarding ways to make HHP an effective strategy in future meat manufacturing.

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Section: Secondary Structurementioning

confidence: 99%

Section: Secondary Structurementioning

confidence: 99%

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Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Liu

et al. 2021

Foods

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“…These changes appear to be due to the weak interaction forces in the original structure of biomacromolecules being changed under F I G U R E 3 Sketch of high hydrostatic pressure (HHP) processing device (a) and mechanisms (b) of extraction and modification of polysaccharides high pressure, including alteration of hydrogen bonds, hydrophobic interactions, and van der Waals forces. The tertiary and quaternary structure of biomacromolecules may encounter reversible and irreversible changes depending upon the holding pressure, treatment time, and temperature (Cepero-Betancourt et al, 2020;Knorr et al, 2006;. The free volume, as a result of the spatial structure of biomacromolecules in the solution, determines the sensitivity of proteins against pressure that is producing a contraction in volume, resulting in the change of stability and functionality of biomacromolecules.…”

Section: Hhp Modification Of Polysaccharidesmentioning

confidence: 99%

Application of nonthermal processing technologies in extracting and modifying polysaccharides: A critical review

Zhang

et al. 2021

Comp Rev Food Sci Food Safe

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Polysaccharides are natural polymer compounds widely distributed in plants, animals, and microorganisms, most of which have a broad spectrum of biological activities to promote human health. They could also be used as texture modifiers in food industry due to their excellent rheological and mechanical properties. Many researchers have shown that nonthermal processing technologies have numerous advantages, such as high extraction efficiency, short extraction time, and environmental friendliness, in the extraction of polysaccharides compared with the traditional extraction methods. Moreover, nonthermal technologies could effectively change the physicochemical properties and structural characteristics of polysaccharides to improve their biological activities or processing properties. Therefore, a comprehensive summary about the extraction and modification of polysaccharides by nonthermal technologies, including ultrasound, high hydrostatic pressure, pulsed electric fields, and cold plasma, was provided in this review. In particular, the underlying mechanisms, processing operations, and current application status of these technologies were discussed. In addition, the applications of combining nonthermal techniques with other technological methods in polysaccharide extraction and modification were briefly introduced.

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“…Tabe et al (2013) reported the palatability and texture of chicken breast were improved after HHP treatment. Cepero‐Betancourt, Opazo‐Navarrete, Janssen, Tabilo‐Munizaga, and Pérez‐Won (2020) studied the effects of HHP on digestibility and protein structure of red abalone ( Haliotis rufescens ).…”

Section: Introductionmentioning

confidence: 99%

Effects of high hydrostatic pressure on color, texture, microstructure, and proteins of the tilapia (Orechromis niloticus) surimi gels

Qin

Ruan

2020

Journal of Texture Studies

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The tilapia (Orechromis niloticus) surimi gels were prepared with high hydrostatic pressure (0, 100, 200, 300, and 400 MPa for 15 min) treatments to investigate the changes in water‐holding capacity, color, gel strength, microstructure, texture, and proteins of the gels. Compared it with cooked gel (40°C/30 min + 90°C/30 min). The whiteness of heat‐induced and HHP‐induced gels were significant (p < .05) higher than that of untreated samples. The gels formed by pressurization were dense and flexible, and formed by cross‐linking based on hydrogen bonding. SDS‐PAGE patterns showed no major change in the actin and tropomyosin protein profiles of gels induced by HHP‐300. Raman spectroscopy confirmed disulfide bonds played an important role in gel formation. A lower intensity ratio observed in HHP‐induced protein supported the tyrosine residues involved in hydrogen bond formation. The changes of secondary structure suggested decreased α‐helix content and increased β‐sheet.

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

Cited by 46 publications

References 45 publications

Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Effects of High Hydrostatic Pressure on the Conformational Structure and Gel Properties of Myofibrillar Protein and Meat Quality: A Review

Application of nonthermal processing technologies in extracting and modifying polysaccharides: A critical review

Effects of high hydrostatic pressure on color, texture, microstructure, and proteins of the tilapia (Orechromis niloticus) surimi gels

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