MYOGLOBIN AS AN ENDOGENOUS INHIBITOR OF PROTEOLYTIC MUSCLE ENZYMES

Citation
Cm. Rosell et al., MYOGLOBIN AS AN ENDOGENOUS INHIBITOR OF PROTEOLYTIC MUSCLE ENZYMES, Journal of agricultural and food chemistry, 44(11), 1996, pp. 3453-3456
Citations number
29
Categorie Soggetti
Food Science & Tenology",Agriculture,"Chemistry Applied
ISSN journal
00218561
Volume
44
Issue
11
Year of publication
1996
Pages
3453 - 3456
Database
ISI
SICI code
0021-8561(1996)44:11<3453:MAAEIO>2.0.ZU;2-6
Abstract
The effect of myoglobin content on the activity of different proteolyt ic systems, lysosomal enzymes, calcium dependent neutral proteinases, and aminopeptidases was examined concretely. Increasing myoglobin cont ent inhibited cathepsin activities (B, B + L, and H). A similar effect was obtained with mu-calpain, which showed about 10% of its initial a ctivity in the presence of 1 mg/mL of myoglobin. In contrast, m-calpai n and calpastatin were almost insensitive to different levels of myogl obin in the medium. Exopeptidases, aminopeptidase B and alanyl aminope ptidase, were inhibited by myoglobin to approximately the same extent as the cathepsins. These results suggest that myoglobin might be consi dered an endogenous inhibitor, which could affect the endogenous prote olytic activity differently in different types of muscles. Consequentl y, the rate of both meat tenderization and generation of free amino ac ids may also be regulated by myoglobin.