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.

Hydroxyapatite and related stationary phases increasingly play a role in the downstream processing of high-value biological materials, such as recombinant proteins, therapeutic antibodies and pharmaceutical-grade plasmid DNA. Chromatographic hydroxyapatite is an inorganic, ceramic material identical in composition, if not in structure, to calcium phosphate found in human bones and teeth. The interaction of hydroxyapatite with biomacromolecules is complex and highly dynamic, which can make predicting performance difficult, but also allows the design of very selective isolation processes. This review discusses the currently commercially available chromatographic materials, different retention mechanisms supported by these materials and differential exploitation for the design of highly specific isolation procedures. The state of the art of antibody purification by hydroxy- and fluoroapatite is reviewed together with tested routines for method development and implementation. Finally, the isolation of plasmid DNA is discussed, since the purification of DNA therapeutics at a sufficiently large scale is an emerging need in bioprocess development and perhaps the area in bioseparation where apatite chromatography can make its most important contribution to date.

Isolation and purification of recombinant proteins, antibodies and plasmid DNA with hydroxyapatite chromatography.

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

Study of the mechanism of interaction of antibody (IgG) on two mixed mode sorbents.

Mixed-mode chromatography sorbents n-hexylamine HyperCel™ (HEA) and phenylpropylamine HyperCel™ (PPA) were evaluated for the study of adsorption of catalase from two different sources. Various parameters such as buffer composition, ionic strength and pH were investigated to study the mechanism of interaction of commercially available pre-purified catalase from Bovine liver, purified catalase from black gram (Vigna mungo) and crude extract of black gram containing catalase with these mixed-mode ligands. A simple and economical screening protocol for identifying optimal buffer conditions for adsorption and desorption of catalase was established with micro volumes of the sorbent in batch mode. With HEA HyperCel, it was observed that pre-purified catalase from both bovine liver and black gram was completely retained at pH 7.0, irrespective of the presence or absence of NaCl in the adsorption buffer, whereas the catalase from crude extract of black gram was completely retained only in the presence of 0.2 M salt in the adsorption buffer. The elution of catalase from both the sources was accomplished by lowering the pH to 4.5 in absence of salt. In case of PPA HyperCel, catalase from both the sources was very strongly adsorbed under different buffer conditions studied, and elution did not yield a significant catalase activity. From the screening experiments, it could be concluded that the interaction of catalase with HEA HyperCel could be dominated by hydrophobic forces with minor contributions from ionic interaction and with PPA HyperCel, it could be a combination of different non-covalent interactions acting on different loci on the surface of the protein.

S. Shiva Ranjini

Papers

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

Study of the mechanism of interaction of antibody (IgG) on two mixed mode sorbents.

Study of catalase adsorption on two mixed-mode ligands and the mechanism involved therein.