Journal
AMINO ACIDS
Volume 46, Issue 7, Pages 1649-1657Publisher
SPRINGER WIEN
DOI: 10.1007/s00726-014-1724-0
Keywords
Nanorods; Papain; Enzyme immobilization; Electrostatic and hydrophobic interactions
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Funding
- University of Hormozgan
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Papain, a thiol protease present in the latex of Carica papaya, is an enzyme which exhibits broad proteolytic activity, and, for this reason, it is utilized in a variety of industrial applications. Immobilization of papain on gold nanoparticles highly preserves its activity and enhances the stability, allowing the reuse of the linked enzyme many times without any significant loss of its catalytic performance. In particular, k (cat) and K (M) values remain substantially unchanged, while immobilized form shows a higher activity on a wider pH range retains 80 % residual activity also at 90 A degrees C and shows higher functionality than the free form when incubated for long time (1 h) at 90 A degrees C and at extreme pH values (3 and 12). A higher activity of immobilized papain with respect to the free form in the presence of various bivalent metal ions, known as strong inhibitors of papain, was also found. The reasons of this enhanced stability of gold nanorods immobilized papain are discussed.
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