EC Number   |
Application |
Reference |
|---|
   3.4.23.1 | analysis |
combined use of a theoretical model that relates electrophoretic behaviour of peptides to their sequence together with capillary electrophoresis-mass spectrometry to characterize the cleavage specificity of recombinant enzymes. Characterization of a protein lysate using recombinant and natural pepsin |
667196 |
| 3.4.23.1 | food industry |
the porcine pepsin digests of cheese whey at a specific acidic pH have the potential to be used as natural food preservatives due to the presence of the three peptides with antibacterial activity against Bacillus subtilis (lactoferrin f(20-30) and beta-lactoglobulin f(14-22)) and Escherichia coli (beta-lactoglobulin f(82-103)) |
754495 |
| 3.4.23.1 | food industry |
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation |
669014 |
| 3.4.23.1 | medicine |
correlation of protein allergen digestion in simulated gastric fluid with that in actual gastric fluid. Digestion of peanut allergen Ara h 1 with pepsin and porcine gastric fluid results in virtually identical hydrolysis patterns |
669034 |
| 3.4.23.1 | medicine |
for elucidation and diagnosis of the allergic potential of egg white ovomucoid, the combination of digestibility studies by simulated gastric fluid and human IgE-binding experiments is useful |
668952 |
| 3.4.23.1 | medicine |
the enzyme is a biomarker of gastric reflux into the esophagus, airways, and lungs |
752496 |
| 3.4.23.1 | nutrition |
modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin, The mutant enzyme F111T/L112F can potentially enhance the rate of solubilization of bovine hide collagen under conditions mild enough to maintain the triple helix structure and hence minimize the rate of subsequent denaturation and proteolytic cleavage |
653827 |
| 3.4.23.1 | nutrition |
role for proteolysis in killing of bacteria. Addition of enzyme alone or in gastric juice at pH 3.5 reduces viability of suspensions of Escherichia coli 690 and K-12 by 100% after 100 min incubation. With Helicobacter pylori, viable counts decrease by 50% after 20 min |
669817 |
| 3.4.23.1 | nutrition |
treatment with pepsin at pH 4.0 results in lowering the (pseudo)peroxidase activity of metmyoglobin both at physiological pH and at meat pH, leading to strongly enhanced prooxidative effect of mildly proteolyzed metmyoglobin on lipid oxidation |
669014 |
| 3.4.23.1 | synthesis |
comparison of hydrolysis kinetics of hemoglobin after immobilization of enzyme on aluminium oxide and on 2-ethanolamine-O-phosphate-modified acidic alumina. Modified alumina results in comparatively less adsorption of peptides and complete adsorption of heme |
668029 |
