Why is peroxidase so widely used

We recorded the slopes of the resulting lines and graphed the average reaction rates y -- here, the dependent variable against the factor being tested x, which was our independent variable. The resulting curves showed the enzyme's optimum value for each factor and what happened to the reaction rate as the conditions moved away from the optimum.

Temperature Effects. Temperature affects all chemical reactions, enzyme-catalyzed or not. In general, higher temperatures equal faster reaction rates. So why did our reaction slow down and eventually stop as we warmed up our test tubes? The optimum temperature for turnip peroxidase fell near room temperature. The optimum temperature probably reflects the soil temperatures in areas where turnips normally grow.

Why such an extreme result? We cooked our enzyme. When you boil an egg, it goes from liquid to solid because the heat breaks and reconfigures the hydrogen bonds between amino-acids in the egg proteins. You permanently change the shape of the proteins, and so permanently change their qualities in this case, texture. The same thing happened to our enzyme. The heat-induced reconfiguration of the hydrogen bonds permanently changed the shape of our enzyme, which caused it to cease functioning.

When the shape of a protein is permanently changed, we say it has been denatured. Graphing Reaction Rates. Aside from curves showing enzyme optima, there is another way to compare reaction rates under varying treatments.

When we graphed our initial reactions on the spectrophotometer, we saw absorbance on the y versus time on the x.

Int J Biological Res 2: Adv Appl Sci Res 3: Water 3: Int J Chem Eng Appli 5: Fungal Biol Rev II International Congress "engineering — Mar Pollut Bull J Appl Microbiol Curr Pharm Biotechnol Int J Biol Res 2: Environ Monit Assess Int J Environ Sci Technol 9: BCBT21 isolated from composting agricultural residual in Vietnam.

Adv Nat Sci Nanosci Nanotechnol 9: J Hazard Mater AIMS Microbiology. Download XML. Export Citation. Article outline. Show full outline. Related pages on Google Scholar on PubMed. Tools Email to a friend. Citation Only. Citation and Abstract. Export Close. Patil SR Production and purification of lignin peroxidase from Bacillus megaterium and its application in bioremediation.

Ganesh P, Dineshraj D, Yoganathan K Production and screening of depolymerising enymes by potential bacteria and fungi isolated from plastic waste dump yard sites.

Pathak VM, Navneet Review on the current status of polymer degradation: a microbial approach. Wei R, Zimmermann W Microbial enzymes for the recycling of recalcitrant petroleum-based plastics: how far are we? Xie X, Chen M, Aiyi Z Identification and characterization of two selenium-dependent glutathione proxidase 1 isoforms from Larimichthys crocea. Niladevi KN Lignolytic enzymes. Veitch NC Horseradish peroxidase: a modern view of a classic enzyme. Husain Q Peroxidase mediated decolorizatio and remediation of wastewar containing industrial dyes: a review.

Nayanashree G, Thippeswamy B Natural rubber degradation by laccase and manganese peroxidase enzymes of Penicillium chrysogenum. Gopi V, Upgade A, Soundararajan N Bioremediation potential of individual and consortium Non-adapted fungal strains on Azo dye containing textile effluent. Bikovens O, Dizhbite T, Telysheva G Characterisation of humin substances formed during co-compositing of grass and wood wastes with animal grease.

Grinhut T, Hadar Y, Chen Y Degradation and transformation of humic substances by saprotrophic fungi: processes and mechanisms. Mojsov K Application of enzymes in the textile industry: a review. Malachite green, a widely-used recalcitrant dye has been confirmed to be carcinogenic and mutagenic against many organisms. Congo red decolorization [ 27 ] Lignin peroxidase isoenzymes LiP 4.

Table 1. Decolorization and detoxification of synthetic, textile dyes, and other industry effluent by microbial peroxidase s. Figure 2. Reaction scheme involved in the production of hydroxyl radical by white rot fungi via quinone redox cycling [ 33 ]. References E. Marco-Urrea, E. Aranda, G. Caminal, and F. Hamid and K. Chanwun, N. Muhamad, N. Chirapongsatonkul, and N. Chandra, A. Abhishek, and M. Huber and B. View at: Google Scholar T. Lundell, M. Hofrichter, R. Ullrich, M.

Pecyna, C. Liers, and T. Marco-Urrea and C. View at: Google Scholar S. Ong, P. Keng, W. Lee, S. Ha, and W. Gopi, A. Upgade, and N. View at: Google Scholar H.

Tien, Z. Salamon, J. Kutnik et al. S1—S30, View at: Google Scholar N. Kirby, G. McMullan, and R. Ng, Q. Cai, C. Wong, A. Chow, and P. Ghasemi, F. Tabandeh, B. Bambai, and K. View at: Google Scholar V. Dawkar, U. Jadhav, S. Jadhav, and S. Krishnaveni and R. View at: Google Scholar F. Pomar, N. Caballero, M. Pedreo, and A. Shin and B. View at: Google Scholar A. Bhunia, S. Durani, and P. View at: Google Scholar P.

Gennaro, A. Bargna, F. Bruno, and G. Bansal and S. View at: Google Scholar Y. Hong, M. Dashtban, S. Chen, R. Song, and W. View at: Google Scholar C. Deivasigamani and N. Kalme, G. Parshetti, S. Du, S. Wang, G. Li et al. Shin, H. Young, and J. Telke, S. Joshi, S. Jadhav, D. Tamboli, and S. Ollikka, K. Alhonmaki, V. Leppanen, T.

Glumoff, T. Raijola, and I. View at: Google Scholar M. Joe, S. Lim, D. Kim, and I. Sugano, Y. Matsushima, and M.

Liers, C. Bobeth, M. Pecyna, R. Ullrich, and M. Faraco, A. Piscitelli, G. Sannia, and P. Kazlauskiene, A. Gefeniene, and R. Mui, W. Cheung, M. Valix, and G. Longoria, R. Tinoco, and R. Hakala, K. Maijala, C. Olsson, and A. Mamatha, A. Vedamurthy, and S. Morales, E. Miki, M.