Production of catalase by fungi growing at low pH and high temperature

Isobe, Kimiyasu; Inoue, Nobuaki; Takamatsu, Yuuki; Kamada, Kazuki; Wakao, Norio

doi:10.1263/jbb.101.73

Cited by 27 publications

(12 citation statements)

References 7 publications

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“…For example, expression of LDS is increased by 1.94-fold under heat stress, which converted oleic acid, linoleic acid, and α-linolenic acid to 7,8-dihydroxy fatty acids, but this enzyme showed no activity when γ-linolenic acid, eicosatrienoic acid, arachidonic acid, and eicosapentaenoic acid were used as substrates ( Brodowskys et al, 1992 ). Catalase, universal in many fungi, rapidly catalyzes the decomposition of hydrogen peroxide into less-reactive gaseous oxygen and water molecules protecting the cell from oxidative damage due to accumulation of ROS ( Isobe et al, 2006 ). In our study, the expression of CAT was not significantly changed under heat stress; however, the expression was significantly lower after recovery.…”

Section: Discussionmentioning

confidence: 99%

iTRAQ-Based Quantitative Proteomic Analysis Reveals Proteomic Changes in Mycelium of Pleurotus ostreatus in Response to Heat Stress and Subsequent Recovery

Zou

Zhang

et al. 2018

Front. Microbiol.

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High temperature is a key limiting factor for mycelium growth and development in Pleurotus ostreatus. Thermotolerance includes the direct response to heat stress and the ability to recover from heat stress. To better understand the mechanism of thermotolerance in P. ostreatus, we used morphological and physiological analysis combined with an iTRAQ-based proteomics analysis of P. ostreatus subjected to 40°C for 48 h followed by recovery at 25°C for 3 days. High temperature increased the concentrations of thiobarbituric acid reactive substances (TBARS) indicating that the mycelium of P. ostreatus were damaged by heat stress. However, these physiological changes rapidly returned to control levels during the subsequent recovery phase from heat stress. In comparison to unstressed controls, a total of 204 proteins were changed during heat stress and/or the recovery phase. Wherein, there were 47 proteins that responded to both stress and recovery conditions, whereas 84 and 73 proteins were responsive to only heat stress or recovery conditions, respectively. Furthermore, quantitative real-time PCR (qRT-PCR) confirmed differential expression of nine candidate genes revealed that some of the proteins, such as a mitogen-activated protein kinase (MAPK), phenylalanine ammonia-lyase (PAL), and heat shock protein (HSP), were also regulated by heat stress at the level of transcription. These differentially expressed proteins (DEPs) in mycelium of P. ostreatus under heat stress were from 13 biological processes. Moreover, protein–protein interaction analysis revealed that proteins involved in carbohydrate and energy metabolism, signal transduction, and proteins metabolism could be assigned to three heat stress response networks. On the basis of these findings, we proposed that effective regulatory protein expression related to MAPK-pathway, antioxidant enzymes, HSPs, and other stress response proteins, and glycolysis play important roles in enhancing P. ostreatus adaptation to and recovery from heat stress. Of note, this study provides useful information for understanding the thermotolerance mechanism for basidiomycetes.

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Section: Discussionmentioning

confidence: 99%

iTRAQ-Based Quantitative Proteomic Analysis Reveals Proteomic Changes in Mycelium of Pleurotus ostreatus in Response to Heat Stress and Subsequent Recovery

Zou

Zhang

et al. 2018

Front. Microbiol.

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“…In the pH 5.0; 6.0; 8,0;9.0 the catalase activity were 211.7 U/mL (77.9%); 237.3 U/mL (87.3%); 249.6 U/mL (91.9); and 234.9 U/mL (86.5%), respectively. Generally, catalase that isolated from fungi stable at range pH 6-9 [12]. Daniel et al [37] reported that catalase-I and catalase-II isolated from Trigonopsis variabilis active in the pH range 3.0 and 10.0 and optimum pH at 5.0 and 8.0, respectively.…”

Section: Optimum Ph and Temperature On Catalase Activitymentioning

confidence: 99%

“…Today, monofuctional catalase have been applied in various industrial fields, such as food and textile [2], [5], [6], analytical fields as a component of different biosensor systems [6], [7], [9], medical [10] and also in energy [11]. Several researches reported that fungi could produce catalase effectively [12], such as: Paracoccidioides brasiliensis has been isolated from yeast cells grown in the presence of 15 mM of hydrogen peroxide and resulted the catalase yield and purity were 79% and 1.3-fold (aceton precipitation), respectively. The molecular weight from this fungi is 244 kDa [13].…”

Section: Introductionmentioning

confidence: 99%

Purification and Characterization of Catalase from Indigenous Fungi of Neurospora crassa InaCC F226

Santoso¹,

Ambarsari²,

Suryani³

et al. 2016

International Journal on Advanced Science, Engineering and Information Technology

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Microbial catalase is an important industrial enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen. This enzyme posseses great potential of application in food, textile and pharmaceutical industries. In this paper, Neurospora crassa InaCC F226 was used to produce catalase. The aim of this research was to purify the catalase producing by Neurospora crassa InaCC F226 using gel filtration column chromatography and characterization of temperature, pH, Vmax, Km and molecular weight. In this study, the Neurospora crassa was cultured on Vogel's medium for 5 days. The cells were harvested in the 50 mM buffer sodium phosphate (pH 7) containing 3% hydrogen peroxide. Supernatant containing crude enzymes of Catalase was separated from cells by centrifugation at 15 minutes on 13000 x g and 4 o C. The purification result using gel filtration was specific activity 1464.9 U/mg, 10.7 fold and 21.7% yield. Characterization of the purified enzyme toward pH and temperature optimum was 7.0 (271.6 U/mL) and 40 o C (286.1 U/mL). The K m and V max found to be 8.8 mM and 5.7 s.mM-1. The catalase activity increased by additiom of Fe +2 , Ca +2 and inhibited by EDTA, Cu +2 and Mn +2. The molecular weight of the catalase was 59.4 kDa.

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“…CAT activity was assayed at 37 °C (Isobe et al 2006) using H 2 O 2 as substrate, GPX activity by NADPH oxidation (monitored at 340 nm) (Nagai et al 2002). AP activity was determined spectrophotometrically (Gonnety et al 2006) using 4-nitrophenyl phosphate as substrate, PPO activity was measured according to Toralles et al (2005) using pyrocatechol as substrate.…”

Section: Methodsmentioning

confidence: 99%

Modulation of enzyme activities of a lead-adapted strain of Rhizopus arrhizus during bioaccumulation of lead

Bhattacharyya

Pal²,

Basumajumdar

2009

Folia Microbiol

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Activity of some enzymes of a Pb-adapted strain of Rhizopus arrhizus augmented significantly during bioaccumulation of Pb from a chemically defined medium. The mycelium of a Pb-adapted strain exposed to 1 microg/mL Pb in a defined medium for 10 d at 28 +/- 2 degrees C exhibited, relative to a wild-type strain, increased activities of antioxidant enzymes, i.e. SOD, CAT and GPX and of enzymes like AP and PPO involved in defense against pathogens. Another response is a significant increase in the cellular thiol content after 4 d. The responses to Pb exposure thus include an increase in the antioxidant and anti-pathogen defense, and an increased metal-chelating ability.

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Production of catalase by fungi growing at low pH and high temperature

Cited by 27 publications

References 7 publications

iTRAQ-Based Quantitative Proteomic Analysis Reveals Proteomic Changes in Mycelium of Pleurotus ostreatus in Response to Heat Stress and Subsequent Recovery

iTRAQ-Based Quantitative Proteomic Analysis Reveals Proteomic Changes in Mycelium of Pleurotus ostreatus in Response to Heat Stress and Subsequent Recovery

Purification and Characterization of Catalase from Indigenous Fungi of Neurospora crassa InaCC F226

Modulation of enzyme activities of a lead-adapted strain of Rhizopus arrhizus during bioaccumulation of lead

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