The Degradation of Bioactive Peptides and Proteins by Dipeptidyl Peptidase IV from Human Placenta

AbstractThe aim of this work was to study the effect of two different pre-treatments, high temperature (100 °C, 5 min) and high pressure (600 MPa, 3 min), on the potential of the enzymes papain, collagenase and Alcalase® to generate bioactive hydrolysates containing dipeptidyl peptidase-IV- (DPP-IV; EC 3.4.14.5) and prolyl endopeptidase- (PEP; EC 3.4.21.26) inhibitory peptides from bovine lung. Both pre-treatments resulted in an increase in the degree of hydrolysis over a 24 h period (P< 0.001) and significantly increased the DPP-IV- and PEP-inhibitory activities of the generated hydrolysates (P< 0.001). Generated hydrolysates included an Alcalase hydrolysate of pressure-treated bovine lung, which was the most active, and showed DPP-IV and PEP half-maximal inhibitory concentration (IC50) values of 1.43 ± 0.06 and 3.62 ± 0.07 mg/ mL, respectively. The major peptides contained in this hydrolysate were determined by liquid chromatography-tandem mass spectrometry, and results demonstrated that bovine lung is a good substrate for the release of bioactive peptides when proper pre-treatment and enzymatic treatment are applied.

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Comparison of plasma dipeptidyl peptidase IV activity in two caiman species: Caiman latirostris and Caiman yacare (Crocodylia, Alligatoridae)

Animal Biology ◽

10.1163/157075511x566524 ◽

2011 ◽

Vol 61 (2) ◽

pp. 199-210 ◽

Cited By ~ 2

Author(s):

María Parachú Marcó ◽

Hugo Ortega ◽

Mark Merchant ◽

Pablo Siroski ◽

Gisela Poletta

Keyword(s):

Significant Positive Correlation ◽

Bioactive Peptides ◽

Plasma Concentrations ◽

Dipeptidyl Peptidase ◽

Dipeptidyl Peptidase Iv ◽

Time Dependent ◽

Strong Positive Correlation ◽

Positive Correlation ◽

Susceptibility To Infection ◽

Physiological Regulator

AbstractDipeptidyl peptidase IV (DPPIV) is a well-characterized protease with broad substrate specificity, functionally-related to the activity of many bioactive peptides. It plays an important role as physiological regulator of a number of peptides that serve as biochemical messengers within the immune system. Plasma DPPIV activity was characterized with respect to temperature, kinetics and concentration dependence in two species of caiman, the broad-snouted caiman (Caiman latirostris) and the black yacare (Caiman yacare). DPPIV activity showed a significant positive correlation from titrations carried out in the presence of different plasma concentrations. DPPIV activity was lower in C. yacare than in C. latirostris at all temperatures tested. C. yacare DPPIV activity showed a significant increase only at higher temperatures whilst C. latirostris plasma demonstrated a strong positive correlation starting at the lowest temperature, probably due to an adaptation for the tolerance of lower temperatures. Exposure of C. latirostris and C. yacare plasma at different time points showed that plasma DPPIV activities were time-dependent, and that the titer-dependent curves were different for the two species. These results revealed that plasma DPPIV activities were different between these two crocodilian species, which could contribute to the differences in susceptibility to infection between them.

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