Role of Central Channel on Catalytic Activity of Scytalidium Catalase | Chapter 6 | Contemporary Research and Perspectives in Biological Science Vol. 9

Catalase, an antioxidant metalloenzyme, primarily functions to decompose hydrogen peroxide into water and molecular oxygen. Catalases have been studied for more than a century. Throughout this period, these enzymes have been identified, purified, and described by many organisms. It has been discovered that catalases currently defined as monofunctional are in fact not monofunctional but also have secondary oxidase/peroxidase activity. For example, the thermophilic fungus Scytalidium thermophilum produces an enzyme catalase parallel to growth, which also has phenol oxidase activity in addition to its primary function. The enzyme was named CATPO (catalase/phenol oxidase) because of its dual activity. To investigate the role of secondary activity in the catalytic mechanism, we focused on the central channel, which is one of the channels leading to the active site and is thought to be involved in oxidative activity. Accordingly, the amino acid in the central channel (T372) was selected as the target for this purpose and a point mutation to A372 was performed. The catalase activity of the T372A variant decreased by 10% compared to the wild type CATPO. Phenol oxidase activity was also reduced by 38% in T372A. The results show that the central channel influences catalytic activity and indicate that the threonine residue is important for activity.

 

Author (s) Details

Elif KALE BAKIR
Department of Biology, Faculty of Arts and Sciences, Kocaeli University, 41001, Kocaeli, Turkey.

 

Bedirhan OZTURK
Department of Biology, Institute of Science, Kocaeli University, 41001, Kocaeli, Turkey.

 

Yonca YUZUGULLU KARAKUS
Department of Biology, Faculty of Arts and Sciences, Kocaeli University, 41001, Kocaeli, Turkey.

 

Please see the book here:- https://doi.org/10.9734/bpi/crpbs/v9/3911

Heavy Metal Chronicles: Assessing Antioxidant Enzyme Activity and Oxidative Stress in Perionyx Excavates Exposed to Contamination | Chapter 9 | Cutting Edge Research in Biology Vol. 9

 This study proposed to investigate the poisonous effects of weighty metals, specifically mercuric chloride, policeman sulfate, zinc sulfate, and their combination, on the endeavor of antioxidant enzymes in the earthworm species Perionyx excavates. The experiment complicated exposing the worms to variable concentrations of the heavy metals. The concentrations of mercuric chloride categorized from 25 to 30 mg/kg of dry soil, copper sulfate concentrations categorized from 60 to 150 mg/kg of dry soil, and zinc sulfate concentrations categorized from 140 to 350 mg/kg of dry soil. The exposure event was set at 5 days. Throughout the experiment, the activities of three antioxidant enzymes, that is to say Superoxide Dismutase (SOD), Catalase (CAT), and Glutathione-S-transferase (GST), were monitored. The results illustrated a dose-weak and time-contingent increase in the activities of these enzymes. Among the difficult metals tested, mercuric chloride shown the highest toxicity at its maximum aggregation. Furthermore, the combination of policeman sulfate and zinc sulfate at their topmost concentrations also presented significant toxicity. In conclusion, this study focal points the detrimental belongings of heavy metal uncovering on the antioxidant enzyme activity in Perionyx excavates. The verdicts emphasize the potential environmental risks associated with sounds that are pleasant contamination and the significance of understanding the biochemical responses of creatures to such contaminants. Further research is warranted to exemplify the underlying mechanisms and enduring consequences of form of rock and roll toxicity in earthworms.

Author(s) Details:

V. V. Vaidya,
Department of Zoology, Smt. S. K. Gandhi Arts, Amolak Science & P.H. Gandhi Commerce College, Kada, Tq. Ashti, Dist. Beed. 414202, India.

Please see the link here: https://stm.bookpi.org/CERB-V9/article/view/11180

Aspergillus fumigatus Catalase | Chapter 3 | Research Advances in Microbiology and Biotechnology Vol. 6

 Catalases are antioxidant enzymes that movement the cleavage of hydrogen whiten into water and molecular oxygen and are widely distributed in type. There is little information in the composition on the kinetic and biochemical properties of catalases created by fungi. Therefore, this study aimed to disengage the catalase enzyme from Aspergillus fumigatus, that is known to be a good catalase builder, and to determine allure properties. Optimal catalase production was worked out on the seventh day of culturing containers grown at 37o C and 155 rpm in excellent-liter YpSs medium containing 1% (w/v) glucose and 0.5 mM H2O2. The catalyst was successfully freed 24-fold with a 55% recovery. The microscopic weight was driven to be ~70 kDa at SDS-PAGE. The optimum reaction temperature of the something which incites activity was set at 60°C and pH at 7.0. Km and Vmax principles were calculated as 7.4 mM and 1250 μ M min-1, individually. Stability tests showed that the something which incites activity could wait active in a wide pH range (4.0-9.0). The warm stability of catalase was 'tween 30o C and 50o C. The enzyme was likewise stable to various solvent such as intoxicating, methanol, acetone, and dimethyl sulfoxide depending on the aggregation and incubation opportunity. The biochemical properties of the something which incites activity (low Km, stability towards various pH and organic solvent, etc.) indicate that A. fumigatus catalase can serve as a good biocatalyst for differing industrial uses.

Author(s) Details:

Ceren Aggez,
Department of Biology, Institute of Natural and Applied Sciences, Kocaeli University, Kocaeli-41001, Turkey.

Yonca Yuzugullu Karakus,
Department of Biology, Faculty of Arts and Sciences, Kocaeli University, Kocaeli-41001, Turkey.

Please see the link here: https://stm.bookpi.org/RAMB-V6/article/view/10920

Role of Different Enzymes in Nectar to Honey Transformations in Indigenous Rockbee, Apis dorsata F. | Chapter 7 | Cutting Edge Research in Biology Vol. 6

 Enzymes form complete part and play decisive duty in biological absorption and systems. The present studies inquire on the role of enzymes namely., invertase, amylase, glucose oxidase and catalase in honey-honey conversion in indigenous rock honey-making Apis dorsata F   during February, 2022 to January 2023. Five stages in metamorphosis of honey from honey of flower comprises decorative nectar (fn), sweetheart crop of foragers (hf), honey crop of building bees (hh), unsealed honey containers (uh) and sealed sweetheart cells (sh). Invertase levels in fn and sh containers were (0.00ml) and (42.40 ml), individually. Similarly, amylase was lowest in the fn (0.00ml) and capital in the sh (16.01 ml). Glucose oxidase levels in fn and sh cells were (0.00ml) and (6.68 ml), individually. Catalase was lowest in the fn (0.00ml) and chief in the sh (4.96 ml). The analysis of difference of invertase and amylase was significant at 1% level (p<0.01), inasmuch as glucose oxidase and catalase was not meaningful at 1% level (p<0.01).The sources of all enzymes, in accordance with the finding, are about the hypopharyngeal, post-cerebral, thoracic, labial, and mandibular glands of foragers and building bees.

Author(s) Details:

M. V. Balasubramanyam,
Department of Zoology, Government First Grade College and PG Centre, Chintamani - 563 125, Bangalore North University, Kolar, India.

Misbhauddin Khan,
Department of Zoology, Government College for Women, Kolar, Bangalore North University, Kolar, India.

Please see the link here: https://stm.bookpi.org/CERB-V6/article/view/10222

Assessment of Catalase Intrinsic Emissions of Electromagnetic Fields as Probable Cause in Cancerogenesis from Consumption of Red and Processed Meat | Chapter 13 | New Horizons in Medicine and Medical Research Vol. 3

 The ubiquitous enzyme catalase is reintroduced and emphasised in this publication as a likely source of cancer genesis in processed meals. Two parts of Prussian Blue Solution (PBS) were combined with two parts of fine iron particles with a diameter of 2000 nanometers (nm). The goal of this paper is to present a theory that links the protein enzyme catalase (CAT), which is introduced to processed meats during the production process, as a possible reason. The International Agency for Research on Cancer issued findings in 2015 warning of a high incidence of cancer linked to the consumption of processed meats. The etiologic factor(s) behind this cancer genesis is (are) unknown at this time. The goal of this paper is to present a hypothesis that links the protein enzyme catalase (CAT), which is added to processed meats during the production process, to a greater cancer incidence. To avoid the "bleaching effect" caused by hydrogen peroxide, CAT is added during the processing of processed foods. Prior investigations linking theorised electromagnetic fields (EMFs) emissions during cell respiration as causing DNA damage and inducing cancer support the hypothesis. That study (CAT) was briefly reported with evidence of electromagnetic fields being emitted (EMFs). The ubiquitous enzyme catalase is reintroduced and emphasised in this publication as a likely cause of cancer genesis linked to processed meat consumption. A Prussian Blue Solution (PBS) was combined with two parts fine iron particles 2000 nanometers (nm) in diameter in additional trials. Human hairs were placed on a slide and subjected to liquid PBS in the control studies. EMFs are emitted by catalase, affecting the metabolic process of the human hair follicle, according to a slide assembly. Because CAT has been proved to be an independent emitter of EMFs, it is thought to be carcinogenic to humans.

Author(S) Details

Abraham A. Embi
13442 SW 102 Lane, Miami, Florida, 33186, USA.

View Book:- https://stm.bookpi.org/NHMMR-V3/article/view/6342

Antioxidant Enzymes in Serum of Patients with Painful Acute Periradicular Abscess: Critical Overview | Chapter 14 | Current Research and Development in Chemistry Vol. 2

The purpose of this study was to compare the pre-treatment and post-treatment serum antioxidants levels in acute periradicular abscess, with pain. Thirty-two patients (18 males, 14 females) with acute and painful endodontic abscesses were included in this study. Before treatment, patients had severe symptoms of inflammation, but at the end of treatment no symptoms of inflammation were observed. Glutathione reductase and catalase activities concentrations were measured in serum of patients with acute periradicular abscess, before and after treatment. There was no statistically significant effect on levels of catalase activity and glutathione reductase concentrations (p > 0.05). 

Author(s) Details

Mehmet Sinan Evcil
Department of Endodontics, Faculty of Dentistry, Atatürk University, 25240 Erzurum, Turkey.

Assoc. Dr. Ismail Uzun
Department of Endodontics, Faculty of Dentistry, Atatürk University, 25240 Erzurum, Turkey.

Prof. Dr. Berna Demircan
 Department of Biochemistry, Medical School, Atatürk University, 25240 Erzurum, Turkey.

Ali Keles
Department of Endodontics, Faculty of Dentistry, Atatürk University, 25240 Erzurum, Turkey.

View Book :- http://bp.bookpi.org/index.php/bpi/catalog/book/173