Document Details

Document Type : Thesis 
Document Title :
RECOMBINANT PRODUCTION AND PROPERTIES OF CELLULASE FROM HYPERTHERMOPHILIC ARCHAEON PYROCOCCUS ABYSSI
الإنتاج المطعم ودراسة خصائص إنزيم السيليوليز المستخلص من بكتيريا آركيون بيروكوكس ابسي المحبة للحرارة العالية
 
Subject : Faculty of Science 
Document Language : Arabic 
Abstract : Cellulose is one of the most abundantly found polysaccharides on the planet earth. The enzyme β-1,4 – endoglucanase or cellulase catalyzes the hydrolysis of β-1,4 glycosidic bond between the glucose molecules in cellulose. The enzyme is not found in human and many animals making them unable to digest cellulose. It is produced by the microbes in the gut of ruminants, where it helps the animals to digest cellulose. The enzyme has applications in the agriculture, biofuel and textile industries. In the present study we have produced a recombinant of cellulase from highly thermophilic archaeon Pyrococcus abyssi. A 1047 bp gene coding for cellulase was PCR amplified and cloned in E. coli using pET21a (+). The gene was expressed in the presence of 0.5mM IPTG. The enzyme was purified by selective heat denaturation of E. coli proteins followed by DEAE-cellulose based anion exchange chromatography. The enzyme was found to have a molecular weight of about 40 kDa on SDS-PAGE. The specific activity of enzyme with CM-cellulose was 1030 U per mg of protein. The optimum pH and temperature for the activity were found 6 and 90°C respectively. In silico studies have shown that the enzyme was found as a monomer. Molecular docking with a few potential protein ligands have shown that Lys256, Asp 177, His 63 are the main active site amino acid residues. 
Supervisor : Dr. Muhammad Shahid Nadeem 
Thesis Type : Master Thesis 
Publishing Year : 1441 AH
2020 AD 
Co-Supervisor : Dr. Mazin A. Zamzami 
Added Date : Tuesday, June 23, 2020 

Researchers

Researcher Name (Arabic)Researcher Name (English)Researcher TypeDr GradeEmail
رضوان محمد الغامديAlghamdi, Radwan MohammedResearcherMaster 

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