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Purification and Thermal Characterization of a Novel Peroxidase from a Local Chick Pea Cultivar

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A novel peroxidase isolated from a local chick pea (Cicer arietinum L.) cultivar (Balksar 2000) was purified by means of ammonium sulfate precipitation, DEAE-cellulose chromatography and two runs on gel filtration. The purified enzyme has a specific activity of 2045 U/mg with 17 % activity recovery. The molecular mass of the enzyme was estimated to be 39 kDa by SDS-polyacrylamide gel electrophoresis. Optimum pH and temperature of the enzyme were 5.5 and 45°C respectively. The thermal denaturation of local chick pea peroxidase was studied in aqueous solution at temperatures ranging from 45°C to 65°C. The temperature of 50&percnt inactivation of the enzyme was found to be 68°C. The enthalpy (ΔH*) and free energy (ΔG*) of thermal denaturation of chick pea peroxidase were 101.4 and 103.4 k J/mol respectively at 65°C.Metals like Zn2+, Mn2+ , Hg2+, Co2+ and Al3+ slightly inhibited the peroxidase activity while Ca2+, Mg2+ and Ba2+ have no effect on enzyme activity. The high specific activity and thermal stability make chick pea peroxidase an alternative to horseradish peroxidase (HRP) in various applications.

Keywords: Chick pea peroxidase; Cicer arietinum L; free energy; purification; thermal denaturation; thermostability

Document Type: Research Article


Affiliations: Industrial Biotechnology Laboratory, Department of Chemistry, University of Agriculture, Faisalabad-38040, Pakistan.

Publication date: August 1, 2006

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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