Reactive species produced in the cell during normal cellular metabolism can chemically react with cellular biomolecules such as nucleic acids, proteins, and lipids, thereby causing their oxidative modifications leading to alterations in their compositions and potential damage to their cellular activities. Fortunately, cells have evolved several antioxidant defense mechanisms (as metabolites, vitamins, and enzymes) to neutralize or mitigate the harmful effect of reactive species and/or their byproducts. Any perturbation in the balance in the level of antioxidants and the reactive species results in a physiological condition called "oxidative stress." A catalase is one of the crucial antioxidant enzymes that mitigates oxidative stress to a considerable extent by destroying cellular hydrogen peroxide to produce water and oxygen. Deficiency or malfunction of catalase is postulated to be related to the pathogenesis of many age-associated degenerative diseases like diabetes mellitus, hypertension, anemia, vitiligo, Alzheimer's disease, Parkinson's disease, bipolar disorder, cancer, and schizophrenia. Therefore, efforts are being undertaken in many laboratories to explore its use as a potential drug for the treatment of such diseases. This paper describes the direct and indirect involvement of deficiency and/or modification of catalase in the pathogenesis of some important diseases such as diabetes mellitus, Alzheimer's disease, Parkinson's disease, vitiligo, and acatalasemia. Details on the efforts exploring the potential treatment of these diseases using a catalase as a protein therapeutic agent have also been described.

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Role of Catalase in Oxidative Stress- and Age-Associated Degenerative Diseases.

After 35 years of development, immobilized metal ion affinity chromatography (IMAC) has evolved into a popular protein purification technique. This review starts with a discussion of its mechanism and advantages. It continues with its applications which include the purification of histidine-tagged proteins, natural metal-binding proteins, and antibodies. IMAC used in conjunction with mass spectroscopy for phosphoprotein fractionation and proteomics is also covered. Finally, this review addresses the developments, limitations, and considerations of IMAC in the biopharmaceutical industry.

Immobilized metal ion affinity chromatography: a review on its applications

Catalase immobilization—A review

Aims: The purpose of this study was to measure antioxidant enzyme (polyphenol oxidase, peroxidase, catalase and superoxide dismutase) activities of crude extract of Rumex obtusifolius L. in order to gain insight about this plant’s antioxidant potential. Study Design: The study was composed of the collection of plant material, extractions of the antioxidant enzymes, activity measurements of the enzymes and finally evaluation of the experimental results. Place and Duration of Study: Department of Chemistry (biochemistry laboratories), Faculty of Science and Arts of Sakarya University, between June 2015 and July 2015. Methodology: Enzymatic antioxidant activity of this plant was investigated by carrying out catalase, superoxide dismutase, peroxidase and polyphenol oxidase enzyme activity assays. Enzyme activities of the crude extract were measured by using spectrophotometric method. Optimum pH and temperature values of each enzyme were also determined for measurement of enzyme activities in ideal conditions. Results: Finally, our results showed that Rumex obtusifolius L. crude extract had good activity for all the enzymatic procedures tested. The activity levels of enzymatic antioxidants polyphenol oxidase, peroxidase, catalase and superoxide dismutase of the plant were found to be 12.8; 195.2; Original Research Article Alici and Arabaci; ARRB, 11(3): 1-7, 2016; Article no.ARRB.29809 2 38.7; 11.6 EU/mL, respectively. Optimum pH and temperature values of all the enzymes (except PPO: optimum temperature 30°C) tested were also foun d to be 7.0 and 25°C, respectively. Conclusion: Our results demonstrate that this edible plant, Rumex obtusifolius L., might be a potential source of natural antioxidants with good antioxidant enzyme capacity.

https://www.journalarrb.com/index.php/ARRB/article/download/25917/48507

Determination of SOD, POD, PPO and CAT Enzyme Activities in Rumex obtusifolius L.

Three-phase partitioning (TPP) was used to purify and recover catalase from potato crude extract. The method consists of ammonium sulfate saturation, t-butanol addition, and adjustment of pH, respectively. The best catalase recovery (262 %) and 14.1-fold purification were seen in the interfacial phase in the presence of 40 % (w/v) ammonium sulfate saturation with 1.0:1.0 crude extract/t-butanol ratio (v/v) at pH 7 in a single step. The sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE) analysis of the enzyme showed comparatively purification and protein molecular weight was nearly found to be 56 kDa. This study shows that TPP is a simple, economical, and quick method for the recovering of catalase and can be used for the purification process.

Sai Srikar Kandukuri

Papers

Purification and characterization of catalase from sprouted black gram (Vigna mungo) seeds.