EC Number   |
Application |
Reference |
|---|
   3.4.14.11 | food industry |
activation of the enzyme is observed after processing at 100-200 MPa and 20-30°C. More intense processing conditions lead to enzyme inactivation. Pressures up to 200 MPa result in a structurally molten globule-like state where PepX maintains its secondary structure but the tertiary structure is substantially affected and enzyme activity increased. Both secondary and tertiary structures are affected severely by higher pressures (450 MPa), which reduce enzyme activity |
-, 753628 |
| 3.4.14.11 | food industry |
during casein hydrolysis, the sequential application of PepX or PepN after prehydrolysis with Alcalase results in an relative degree of hydrolysis (rDH) increase of 1.12- or 2.00fold, respectively, compared to only using Alcalase. The simultaneous application of Alcalase, PepX and PepN from the beginning shows similar results as the sequential application, but only three remaining peptides are observed and the hydrolysis time is reduced from 16 h (sequential approach) to 6.5 h (simultaneous approach) |
-, 753467 |
| 3.4.14.11 | food industry |
immobilization of enzyme as cross-linked enzyme aggregate CLEA results in 66% residual activity at 50°C after 4 d (compared to 50% for the free enzyme), and the optimum temperature increases from 30°C for wild-type to 40°C for PepN-CLEAs. With combined CLEAs of PepX/PepN the highest activity yield is about 18% and 9% for PepX and PepN activity, respectively. The combined CLEAs are suitable for application in protein hydrolysis. The relative degree of hydrolysis is increased by approximately 52% compared to an alcalase pre-hydrolyzed casein solution |
-, 752634 |
| 3.4.14.11 | food industry |
production, characterization and use of cross-linked enzyme aggregates (CLEAs) from a fusion protein of PepN and PepX (FUS-PepN_PepX CLEA). The FUS-PepN_PepX CLEAs produced have activity for both specific enzymes. pH and temperature optima, environmental conditions show that the CLEAs are suitable for application in a complex matrix, such as food protein hydrolysates. The relative degree of hydrolysis of a prehydrolyzed casein solution is increased by 100% and the hydrolysate obtained shows a strong antioxidative capacity (ABTS-IC50 value: 7.85 microg/ml) |
-, 753465 |
| 3.4.14.11 | food industry |
X-prolyl dipeptidyl aminopeptidase PepX, EC 3.4.14.11, and the general aminopeptidase N, EC 3.4.11.2, exhibit a clear synergistic effect in casein hydrolysis studies. Here, the relative degree of hydrolysis is increased by approx. 132% |
-, 732739 |
| 3.4.14.11 | synthesis |
comparison of the effects of cell disruption methods on the activity of PepX. The optimized values of high-pressure homogenization are one cycle at 130 MPa providing activity of 114.47 mU/ml, while sonication gives an activity of 145.09 mU/ml at 28 min with 91% power and three cycles |
-, 755630 |
