Quality and proteome changes of beef M.longissimus dorsi cooked using a water bath and ohmic heating process

Tian, Xiaojing; Wu, Wei; Yu, Qunli; Hou, Man; Jia, Fei; Li, Xingmin; Dai, Ruitong

doi:10.1016/j.ifset.2016.02.013

Cited by 67 publications

(30 citation statements)

References 46 publications

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“…In terms of MS results, the heat treatment clearly resulted in a lower number of peptide identifications and sequence coverage for these 3 proteins (the 2 myosin light chains and the tropomyosin alpha‐chain), but this was not the case for the actin and myoglobin. A similar proteomic approach has also been applied to investigate protein changes of ohmically cooked beef (Tian and others ). The work by Tian and others () indicated that the ohmic cooking led to less protein damage compared to the water bath cooking, as the ohmically cooked samples exhibited overall more protein spots with relatively higher abundance.…”

Section: Protein Structure Modifications In Meat As a Results Of Cookingmentioning

confidence: 99%

“…A similar proteomic approach has also been applied to investigate protein changes of ohmically cooked beef (Tian and others ). The work by Tian and others () indicated that the ohmic cooking led to less protein damage compared to the water bath cooking, as the ohmically cooked samples exhibited overall more protein spots with relatively higher abundance.…”

Section: Protein Structure Modifications In Meat As a Results Of Cookingmentioning

confidence: 99%

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Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

175

115

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Food ingredients commonly undergo heat treatment. Meat, in particular, is typically consumed after some form of heating, such as boiling or roasting. Heating of meat can introduce a wide range of structural changes in its proteinaceous components. At the 3-dimensional structural level, meat proteins may denature and form aggregates upon heating. At the molecular level, primary structure (amino acid residue) alterations reported in cooked meat include protein carbonylation, modification of aromatic residues, and the formation of Maillard reaction products. Identification of these modifications is essential for determining the mechanism of thermal processing of meat and allowing better control of the nutritional and functional properties of products. This article reviews and summarizes the current state of understanding of protein modifications at the molecular level in commonly consumed mammalian food. In addition, relevant case studies relating to characterization of heat-induced amino acid residue-level modifications in other biological materials such as milk and wool are discussed to provide complementary insights.

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Section: Protein Structure Modifications In Meat As a Results Of Cookingmentioning

confidence: 99%

Section: Protein Structure Modifications In Meat As a Results Of Cookingmentioning

confidence: 99%

Cooking‐Induced Protein Modifications in Meat

Morton

Clerens

et al. 2016

Comp Rev Food Sci Food Safe

175

115

View full text Add to dashboard Cite

show abstract

“…Tian and co-workers compared the impact of OH processing and conventional water bath cooking on beef muscle. Due to its fast and homogeneous heating, OH provides a limited time for the denaturation and aggregation of muscle fibres and connective tissues, thus resulting in a beef product with a significantly lower shear force value, which was reflected in higher tenderness (Tian et al, 2016). Furthermore, in highly processed fish products as surimi, OH leads to a maximization of the gel functionality due to its associated fast heating rates (Yongsawatdigul, Park, Kolbe, Dagga, & Morrissey, 1995).…”

Section: Quality and Safety Aspectsmentioning

confidence: 99%

Electric field effects on proteins – Novel perspectives on food and potential health implications

Rodrigues

Avelar

Machado

et al. 2020

Food Research International

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Electric fields (EF) technologies have been establishing a solid position in emergent food processing and have seen as serious alternatives to traditional thermal processing. During the last decades, research has been devoted to elucidation of technological and safety issues but also fundamental aspects related with interaction of electric fields (EF) with important macromolecules, such as proteins. Proteins are building blocks for the development of functional networks that can encompass health benefits (i.e. nutritional and bioactive properties) but may be also linked with adverse effects such as neurodegenerative diseases (amyloid fibrils) and immunological responses. The biological function of a protein depends on its tridimensional structure/conformation, and latest research evidences that EF can promote disturbances on protein conformation, change their unfolding mechanisms, aggregation and interaction patterns. This review aims at bringing together these recent findings as well as providing novel perspectives about how EF can shape the behavior of proteins towards the development of innovative foods, aiming at consumers' health and wellbeing.

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“…The main features of this new thermal processing are short processing time, as the heat is generated internally, no need to heating medium, no hot or overheated surface, and no temperature gradient (Erdogdu et al 2018;Jaeger et al 2016). A wide number of studies have been focused on the advantages of ohmic heating over conventional thermal processing, such as water bath (Dai et al 2014;Tian et al 2016Tian et al , 2020 and frying pan (Ángel-Rendón et al 2019). Indeed, the previous studies reported that ohmic-treated pork batters and short shank samples presented several benefits, including (i) shorter cooking times, (ii) more uniform temperatures, and (iii) lower cooking loss compared to those treated with the other cooking methods.…”

Section: Ohmic Heatingmentioning

confidence: 99%

Monitoring Thermal Treatments Applied to Meat Using Traditional Methods and Spectroscopic Techniques: a Review of Advances over the Last Decade

Hassoun

Aït‐Kaddour

Sahar

et al. 2020

Food Bioprocess Technol

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Thermal treatments are often applied during processing or preparation of muscle foods aiming to both improve the palatability and organoleptic properties and to ensure the safety of the treated food. However, the application of inappropriate or severe thermal treatments can lead to undesirable changes in the sensory and nutritional quality of heat-processed products, and especially so for foods that are sensitive to thermal treatments, such as meat and meat products. The impact of traditional and new heat processing technologies (e.g. microwaving, ohmic, and radio frequency heating) on meat quality has been widely assessed by a wide range of conventional methods, such as sensory, microbiological, and physicochemical methods. Due to the destructive nature and the time required to perform these assessments, alternative online methods are highly needed in order to achieve continuous monitoring through online applications. In this review paper, both traditional and new heat processing methods and their impact on the quality of meat will be first briefly presented. The methods and techniques that have been applied to monitor changes induced by application of thermal treatments will be then discussed. The main focus will be put on the application of spectroscopic techniques, as rapid and non-destructive methods compared to most conventional techniques. Finally, future trends and possible applications and research directions will be suggested.

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Quality and proteome changes of beef M.longissimus dorsi cooked using a water bath and ohmic heating process

Cited by 67 publications

References 46 publications

Cooking‐Induced Protein Modifications in Meat

Cooking‐Induced Protein Modifications in Meat

Electric field effects on proteins – Novel perspectives on food and potential health implications

Monitoring Thermal Treatments Applied to Meat Using Traditional Methods and Spectroscopic Techniques: a Review of Advances over the Last Decade

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