2016
DOI: 10.1111/1541-4337.12243
|View full text |Cite
|
Sign up to set email alerts
|

Cooking‐Induced Protein Modifications in Meat

Abstract: 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, an… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1
1
1

Citation Types

2
115
0
1

Year Published

2017
2017
2024
2024

Publication Types

Select...
7

Relationship

0
7

Authors

Journals

citations
Cited by 173 publications
(127 citation statements)
references
References 184 publications
2
115
0
1
Order By: Relevance
“…Myofibrillar and connective tissue proteins (collagen and elastin) control the toughness of muscle tissues. During heating, these proteins are denatured, causing destruction of cell membranes, shrinkage of fibers, aggregation, and gelling of myofibrillar and sarcoplasmic proteins, and shrinkage and solubilization of connective tissue (Tornberg ; Yu and others ). Thus, cooked meat is easier to chew, digest, and is, therefore, more nutritious than uncooked meat.…”
Section: Impact Of Cooking On the Nutritional Properties Of Meat And mentioning
confidence: 99%
“…Myofibrillar and connective tissue proteins (collagen and elastin) control the toughness of muscle tissues. During heating, these proteins are denatured, causing destruction of cell membranes, shrinkage of fibers, aggregation, and gelling of myofibrillar and sarcoplasmic proteins, and shrinkage and solubilization of connective tissue (Tornberg ; Yu and others ). Thus, cooked meat is easier to chew, digest, and is, therefore, more nutritious than uncooked meat.…”
Section: Impact Of Cooking On the Nutritional Properties Of Meat And mentioning
confidence: 99%
“…(a, b)). This result indicated that heating caused protein denaturation, during which more free SH groups were exposed . Heating at higher temperature (100 °C) should have induced faster formation of disulfide bonds and reduced the level of total SH groups, compared with the control sample and the sample that was heated at 70 °C.…”
Section: Resultsmentioning
confidence: 94%
“…However, cross‐links may be formed in proteins by other mechanisms, via the oxidation of two cysteines leading to the formation of disulfide bonds and the aforementioned dityrosines . The benefits of the inhibition of Schiff base formation may also be emphasized given the role of these structures in the functionality and digestibility of meat proteins . Considering the fact that this is the first study involving the analysis of protein oxidation in a wine‐based meat marination system with thermal application, the mechanisms of how the interactions between meat proteins and specific phenolic compounds occurs need to be further clarified.…”
Section: Resultsmentioning
confidence: 99%
“…The oxidation of proteins in cooked meat has become a topic of scientific and technological interest owing to its influence on food quality and consumer safety. 35,36 The influence of wine marination of lipid oxidation has already been studied, and expected antioxidant effects were found. 18 Conversely, the present study investigated the effect of wine-based marination on protein oxidation.…”
Section: Protein Oxidation In Roasted Strip Steaks As Affected By Marmentioning
confidence: 99%