Document Details

Document Type : Thesis 
Document Title :
EXTRACTION AND PURIFICATION OF OXIDO-REDUCTIVE ENZYME (PREOXIDASE) FROM HUMMAYD (RUMEX VESICARIUS) AND IMMOBILIZATION ON NANOMATERIALS
إستخلاص وتنقية إنزيم الأكسدة والأختزال (بيروكسيداز) من الحميض (Rumex vesicarius) وتحميله على جسيمات نانوية
 
Subject : Faculty of Science 
Document Language : Arabic 
Abstract : One of the most prominent functions of the enzyme as a natural biocatalyst is its ability to improve the rate of chemical reactions inside a cell. Peroxidases having the ability to bioremediate wastewater that has been polluted with cresols, chlorinated phenols, and phenols. Rumex vesicarius is frequently used to heal toothaches, stomach heat, and it also increases appetite. The Rumex vesicarius are consumed to treat indigestion, constipation, and jaundice. The objectives of this research are to identify novel peroxidase sources, investigate the biochemical properties of enzymes, and develop immobilization techniques for the reuse of enzymes across a large number of reaction cycles. Sigma-Aldrich, DEAE-Sepharose, Fe3O4, and CMC magnetic nanoparticles were used in addition to analytical-grade compounds. Specimens of Hummayd (Rumex vesicarius L.) were obtained. The quantity of enzyme required to raise the optical density by 1.0 per minute is considered one unit of activity. The subunit purity and molecular mass of the isolated enzyme were also calculated using SDS-PAGE. Peroxidase diluted in 50 mM sodium acetate buffer pH 4.0 was immobilized on Fe3O4 magnetic nanoparticles by turning them end over end for one night at room temperature. PerkinElmer spectrum 100 FT-IR spectrometer was used to collect sample FTIR spectra. Km values were determined by preparing Line-weaver-Burk plots with varying amounts of guaiacol and H2O2 as substrates. The results revealed two peaks with Rumex vesicarius peroxidase activity designated as POD I and POD II which has 1.3- and 0.2-fold purification over the crude extract respectively. Furthermore, POD I purification revealed 2 peroxidase activity: POD IA and POD IB with activities of 23 and 116 units/mg protein, respectively. Immobilization efficiency of Fe3O4 was enhanced and the activity after 10 reuses; the immobilized enzyme retained 53% of its initial activity. Keywords: Enzyme, Peroxidase, Immobilization, Nanoparticles, Rumex vesicarius 
Supervisor : Dr. Faisal Al-Zahrani 
Thesis Type : Master Thesis 
Publishing Year : 1445 AH
2023 AD 
Added Date : Tuesday, November 14, 2023 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
عبدالرحمن سعود الفهيديAl Fahidi, Abdul Rahman SaudResearcherMaster 

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