کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1186294 | 963432 | 2010 | 8 صفحه PDF | دانلود رایگان |

The stability and catalytic activity of bovine cathepsin D in Bis-Tris buffer (pH 6.0) in different pressure–temperature domains (0.1–650 MPa, 20–75 °C) were investigated and described with mathematical models. Cathepsin D inactivation followed first-order kinetics at all pressure–temperature conditions tested. The protease was largely pressure stable at room temperature and heat stable at ambient pressure up to 300 MPa and 55 °C, respectively, causing less than 10% inactivation after 10 min treatment. Pressure and temperature act synergistically on the enzyme inactivation under most conditions. However, at 100 MPa a significant stabilisation of the enzyme against temperature-induced inactivation was observed. Pressure drastically inhibited the cleavage of a synthetic substrate by cathepsin D in Bis-Tris buffer (pH 6.0) causing a reduction of the catalytic rate of more than 50% at 100–400 MPa. Maximal substrate cleavage by cathepsin D was identified at 60 °C and ambient pressure conditions after 20 min treatment.
Journal: Food Chemistry - Volume 120, Issue 2, 15 May 2010, Pages 474–481