J. L GRAY’s research while affiliated with Michigan State University and other places

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Publications (1)


Possible role of muscle protein in flavor and tenderness of meat
  • Article

February 2007

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33 Reads

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12 Citations

A. M. PEARSON

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ARLENE M. WOLZAK

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J. L GRAY

Evidence suggests that both the myofibrillar proteins and collagen play important roles in meat flavor and tenderness. The probable contributions of the purified proteins to flavor are reviewed in terms of their amino acid composition, especially the sulfur containing and certain other amino acids that have been implicated in meat flavor development. Myofibrils solubilized in sodium dodecylsulfate (SDS) undergoproteolysis on warming to room temperature overnight or on storing for several days at 0–4°C as demonstrated by extra protein bands. The extra proteins appear to be due to the presence of indigenous muscle proteases. The implications of some indigenous muscle proteases are reviewed in terms of their probable role in tenderization of postmortem meat.

Citations (1)


... The flavor of dry-cured products, Coppa Piacentina PDO included, is based on a pool of different volatile and non-volatile compounds which are produced also during the ripening step (Sforza et al., 2006). Non-volatile molecules include peptides and free amino acids, which are released from the muscle proteins by the action of endopeptidases, mainly calpains and cathepsins, and exopeptidases (Pearson et al., 1983). The pool of these proteinaceous compounds directly contributes to the final taste, and indirectly to certain aroma compounds (Toldrá, 2006). ...

Reference:

Volatile compounds, gamma-glutamyl-peptides and free amino acids as biomarkers of long-ripened protected designation of origin Coppa Piacentina
Possible role of muscle protein in flavor and tenderness of meat
  • Citing Article
  • February 2007