A. della Malva
University of Foggia
28 Papers
12 Citations
A. della Malva is an academic researcher from University of Foggia. The author has contributed to research in topics: Biology & Chemistry. The author has an hindex of 8, co-authored 10 publications.
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Papers
Proteolytic pattern of myofibrillar protein and meat tenderness as affected by breed and aging time.
TL;DR: Data suggest that tenderness and proteolytic changes during aging are related to animal's breed.
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Changes in meat quality traits and sarcoplasmic proteins during aging in three different cattle breeds.
Rosaria Marino,Marzia Albenzio,A. della Malva,Mariangela Caroprese,Antonella Santillo,Agostino Sevi +5 more
TL;DR: Protein identification and western blotting showed the presence of myosin light chains, Troponin T and tropomyosin proteins during aging, suggesting a degradation of myofibers and a more intense proteolysis especially in the Podolian breed.
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Proteolytic changes of myofibrillar proteins in Podolian meat during aging: focusing on tenderness.
TL;DR: Data highlight that aging affects the meat tenderness and proteolysis with different intensities in each muscle and could be useful for the development of muscle specific strategies for improving the quality and value in different commercial cuts.
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Effect of low voltage electrical stimulation on protein and quality changes in bovine muscles during postmortem aging
Yuan H. Brad Kim,Steven M. Lonergan,J. K. Grubbs,S.M. Cruzen,Aaron N. Fritchen,A. della Malva,Rosaria Marino,E. Huff-Lonergan +7 more
TL;DR: The data confirmed that low voltage ES at 90 min of exsanguination had no effect on proteolysis and tenderness development in the longissimus dorsi, semimembranosus, adductor or gracilis in beef.
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Identification of peptides in functional Scamorza ovine milk cheese
Marzia Albenzio,Antonella Santillo,Rosaria Marino,A. della Malva,Mariangela Caroprese,Agostino Sevi +5 more
TL;DR: Peptides obtained from reverse phase-HPLC water-soluble extract of Scamorza cheeses were analyzed and identified fragments showed encrypted peptide sequences that shared structural homology with previously described bioactive peptides in ovine milk and dairy products.
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