- Tytuł:
- Muscle cathepsins of marine fish and invertebrates
- Autorzy:
-
Kolodziejska, I.
Sikorski, Z.E. - Powiązania:
- https://bibliotekanauki.pl/articles/1372835.pdf
- Data publikacji:
- 1995
- Wydawca:
- Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
- Tematy:
-
invertebrate
endopeptidase
fish
structure
protease
extracellular matrix
lysosome
exopeptidase
cathepsin C
cathepsin A
muscle protein
myofibrillar protein
lysosomal protease
marine fish
protein
myofibril
muscle cathepsin
food preservation
sarcoplasm
cathepsin L
carboxypeptidase A
cathepsin B - Opis:
- Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.
- Źródło:
-
Polish Journal of Food and Nutrition Sciences; 1995, 04, 3; 3-10
1230-0322
2083-6007 - Pojawia się w:
- Polish Journal of Food and Nutrition Sciences
- Dostawca treści:
- Biblioteka Nauki
Artykuł