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Effect of sodium, potassium, calcium and magnesium chloride salts on porcine muscle proteases
- Source :
- European Food Research and Technology. 229:93-98
- Publication Year :
- 2009
- Publisher :
- Springer Science and Business Media LLC, 2009.
-
Abstract
- This study is focused on the effect of sodium chloride alternative salts (KCl, MgCl2 and CaCl2) on porcine muscle proteases (cathepsins, dipeptidylpeptidases and aminopeptidases). In general, KCl exerted a very similar effect to NaCl for all the studied enzymes, while the effect of divalent salts (CaCl2 and MgCl2) was more pronounced. Cathepsins, dipeptidyl peptidase III, dipeptidyl peptidase IV and alanyl aminopeptidase activities were strongly inhibited by all the chloride salts especially by divalent ones. Dipeptidyl peptidase II and leucyl aminopeptidase were little affected and methionyl aminopeptidase was only inhibited by divalent salts. Dipeptidyl peptidase I was strongly activated by low concentrations of the chloride salts except NaCl. Arginyl aminopeptidase was activated by NaCl and KCl and low amounts of MgCl2, while CaCl2 showed a strong inhibitory effect. This is very important as these enzymes play important roles in dry-cured meats and their activity is, in general, regulated by sodium chloride. Thus, reductions in the sodium concentration with subsequent increases of other alternative cations may have relevant consequences on enzyme activity that should be taken into account when processing dry-cured meats.
- Subjects :
- inorganic chemicals
chemistry.chemical_classification
Sodium
Methionyl aminopeptidase
chemistry.chemical_element
General Chemistry
Calcium
Biochemistry
Chloride
Industrial and Manufacturing Engineering
Dipeptidyl peptidase
Cathepsin C
Divalent
chemistry
medicine
Leucyl aminopeptidase
Food Science
Biotechnology
medicine.drug
Subjects
Details
- ISSN :
- 14382385 and 14382377
- Volume :
- 229
- Database :
- OpenAIRE
- Journal :
- European Food Research and Technology
- Accession number :
- edsair.doi...........91f9c6452d836a45b9f356a54c6a8129
- Full Text :
- https://doi.org/10.1007/s00217-009-1029-9