Changes in Structures and Properties of Collagen Fibers during Collagen Casing Film Manufacturing

Liu, Fei; Yu, Zhe; Wang, Beibei; Chiou, Bor-Sen

doi:10.3390/foods12091847

Cited by 9 publications

(1 citation statement)

References 22 publications

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“…They concluded that changes in the concentration and ratio of different proteins of whey protein isolate could lead to changes in the denaturation and aggregation behavior of complex systems, such as whey protein isolate. Liu et al [50] studied changes in the structures and properties of collagen fibers during collagen casing film manufacturing and found that dried collagen casing had the lowest enthalpy value and the lowest thermal denaturation temperature; this indicated that the thermal stability of the new structure was clearly inferior to the natural structure of the raw material, and similar protein destabilization has been found in this study.…”

Section: Discussionsupporting

confidence: 79%

Thermal Characterisation and Isoconversional Kinetic Analysis of Osmotically Dried Pork Meat Proteins Longissimus dorsi

Ostojić

Micić

Zlatanović

et al. 2023

Foods

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The kinetic properties and thermal characteristics of fresh pork meat proteins (Longissimus dorsi), as well as osmotically dehydrated meat proteins, were investigated using differential scanning calorimetry. Two isoconversional kinetical methods, namely the differential Friedman and integral Ortega methods, were employed to analyze the data. The obtained kinetic triplet, activation energy, pre-exponential factor, and extent of conversion, has been discussed. The resulting activation energy for proteins of fresh meat ranges between 751 kJmol−1 for myosin, 152 kJmol−1 for collagen and sarcoplasmic proteins, and 331 kJmol−1 for actin at a conversion degree of 0.1 to 0.9. For osmotically dried pork meat proteins, the values range from 307 kJmol−1 for myosin 272 kJmol−1 for collagen and sarcoplasmic proteins, and 334.83 kJmol−1 for actin at a conversion degree from 0.1 to 0.9. The proteins of the dry meat obtained by osmotic dehydration in molasses could be described as partly unfolded as they retain the characteristic protein denaturation transition. Concerning the decrease in enthalpies of proteins denaturation, thermodynamic destabilization of dried meat proteins occurred. On the contrary, dried meat proteins were thermally stabilized with respect to increase in the temperatures of denaturation. Knowledge of the nature of meat protein denaturation of each kind of meat product is one of the necessary tools for developing the technology of meat product processing and to achieve desired quality and nutritional value. The kinetic analysis of meat protein denaturation is appropriate because protein denaturation gives rise to changes in meat texture during processing and directly affects the quality of product.

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Section: Discussionsupporting

confidence: 79%