Thermal denaturation of proteins in the muscle fibre and connective tissue from bovine muscles composed of type I (masseter) or type II (cutaneous trunci) fibres: DSC and FTIR microspectroscopy study

•Cooking decreased α- helix, increased aggregates in muscle fibre and IMCT proteins.•Greater denaturation of myosin in cutaneous trunci than in masseter at

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Bibliographic Details
Published in:Food chemistry 2021-05, Vol.343, p.128544-128544, Article 128544
Main Authors: Vaskoska, Rozita, Vénien, Annie, Ha, Minh, White, Jason D., Unnithan, Ranjith R., Astruc, Thierry, Warner, Robyn D.
Format: Article
Language:English
Subjects:
Animals
Beef
Calorimetry, Differential Scanning
Cattle
Connective Tissue - chemistry
Cooking
DSC
Fibre type
Food and Nutrition
FTIR
Life Sciences
Meat
Microspectroscopy
Muscle Proteins - chemistry
Muscle Proteins - isolation & purification
Protein denaturation
Protein Structure, Secondary
Spectroscopy, Fourier Transform Infrared
Temperature
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Description
Summary:•Cooking decreased α- helix, increased aggregates in muscle fibre and IMCT proteins.•Greater denaturation of myosin in cutaneous trunci than in masseter at
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2020.128544