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Information Journal Paper

Title

STRUCTURAL STUDY ON PEPSIN STABILITY IN THE PRESENCE OF ZNO AND FE3O4 NANOPARTICLES

Pages

 Start Page 344 | End Page 351

Keywords

ZNO AND FE3O4 NANOPARTICLESQ2

Abstract

 Porcine PEPSIN A (EC 3.4.23.1), belongs to the aspartic protease family, and is secreted as a zymogen called PEPSINogen. PEPSINogen activation occurs at pH values between 1 and 4. PEPSIN consists of a bilobal conformation with two catalytic aspartic residues (Asp32 and Asp215) on either side of the active site, The structure of porcine PEPSIN is predominantly b-strand and random coil with limited a-helix. Porcine PEPSIN is most efficient cleaving peptide bonds between hydrophobic and preferably aromatic amino acids such as phenylalanine, tryptophan, and tyrosine. Because the importance of PEPSIN enzyme as an industrial enzyme in the food industry and nano particles functions in industry, we investigated STRUCTURAL STABILITY of PEPSIN in presence and absence of ZnO and Fe3O4 nanoparticles. This study were performed using glycin-Hcl (0.1M) buffer at pH=2 and temperature range (303 to 363) K. porcine PEPSIN stability Was not changed in the presence of Zno and Fe3O4 nanoparticles. Strength of the electrostatic and hydrogen interactions between PEPSIN enzyme and ZnO, Fe3O4 nanoparticles Were a low level in DENATURATION of PEPSIN.

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