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Proteolysis in muscle tissues during the processing of dry-cured ham

Marina Krvavica
Andrijana Lukić
Marija Vrdoljak
Jelena Đugum ; Ministarstvo poljoprivrede, šumarstva i vodnog gospodarstva, Grada Vukovara 78, Zagreb
Duška Ćurić ; Prehrambeno biotehnološki fakultet Sveučilišta u Zagrebu, Zavod za prehrambeno-tehnološko inženjerstvo, Pierottijeva 6, Zagreb


Puni tekst: hrvatski pdf 535 Kb

str. 221-229

preuzimanja: 1.125

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Sažetak

Proteolysis is a complex biochemical process of hydrolysis of proteins to the peptides and free amino acids by endogenous enzymes action. By action of muscle proteases, which are endopeptidases (calpains and catepsins) responsible for muscle tissue initially tenderization as well as egzopeptidases (peptidases, aminopeptidases and carboxipeptidases) responsible for later stages of proteolytical degradation, the post mortem muscle proteins breakdown take place. Proteolysis in muscle starts with releasing of Ca2+ ions from the sarcoplasmic reticulum and activation of calpains which are probably responsible for Z-disc and regulatory proteins degradation, and it proceeds by activation of catepsins and main myofibrillarproteins degradation which calpains are unable to hydrolyse. Proteins degradation post mortem and increment of meat pH as well as increment of salt concentration inactivate the calpains just after 10 to 14 days after the slaughtering. These processes produce the protein fragments and middle polypeptides. Further polypeptides and oligopeptides degradation until the small peptides and free amino acids takes place by action of different egzopeptidases (tripeptidylpeptidases, dipeptidylpeptidases, dipeptidases, aminopeptidases and carboxipeptidases). The products of proteolysis have a direct influenceondry-curedhamtexture and taste as well, and they ere involved in creating of characteristic flavouranddry-cured ham final sensorial characteristics.

Ključne riječi

proteolysis, dry-cured ham

Hrčak ID:

21287

URI

https://hrcak.srce.hr/21287

Podaci na drugim jezicima: hrvatski

Posjeta: 2.577 *