Thermostability of cardosin A from Cynara cardunculus L.

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Thermostability of cardosin A from Cynara cardunculus L

The structural stability of cardosin A, a plant aspartic proteinase (AP) from Cynara cardunculus L., has been investigated by high-sensitivity differential scanning calorimetry, intrinsic fluorescence and circular dichroism spectroscopy, and enzymatic activity assays. Even though the thermal denaturation of cardosin A is partially irreversible, valid thermodynamic data can be obtained within a ...

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The enzymatic hydrolysis of the major whey proteins, namely b-lactoglobulin (b-Lg) and a-lactalbumin (a-La), was experimentally studied using whey as substrate; an aspartic protease (cardosin A), previously extracted from the flowers of Cynara cardunculus and purified by gel filtration and ion exchange chromatographies, was used for this purpose. Sweet whey was incubated for 24 h at various enz...

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ژورنال

عنوان ژورنال: Thermochimica Acta

سال: 2003

ISSN: 0040-6031

DOI: 10.1016/s0040-6031(02)00613-5