Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei

Chambergo, Felipe S.; Valencia, Estela Y.; Ferreira-Junior, Jose Ribamar; Camilo, César M.; Campana, Patricia T.

doi:10.1016/j.ijbiomac.2011.09.015

Cited by 10 publications

(9 citation statements)

References 50 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bacteria were able to express the proteins TrSOD, TAT‐TrSOD‐Yfp, and Ab‐TrSOD under the used conditions. These results corroborate the data from Chambergo et al 19 . and Fontolan 46 who also obtained TrSOD expression upon induction with IPTG.…”

Section: Resultssupporting

confidence: 92%

“…18 Even so, the use of SOD in its free form has some disadvantages, such as enzyme instability and low cell uptake. 18 In this scenario, Chambergo et al 19 characterized a MnSOD enzyme from the fungus Trichoderma reesei (TrSOD), which showed stability between temperatures of 30-90 • C for up to 1 h and activity in pH between 2.6 and 9.0. However, cell uptake is still a barrier to be overcome, since the plasma membrane limits the entry of macromolecules.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Delivery of superoxide dismutase by TAT and abalone peptides for the protection of skin cells against oxidative stress

Reigado

Adriani

Santos

et al. 2022

Biotech and App Biochem

View full text Add to dashboard Cite

Trichoderma reesei superoxide dismutase (TrSOD) is a well-characterized enzyme being stable between 30 and 90 • C for 1 h with activity at pH between 2.6 and 9.0. This work aimed to clone, express, purify, and evaluate the protective effect antioxidant of this enzyme on skin cells when fused to transactivator of transcription (TAT) protein transduction domain of HIV-1 and abalone (Ab) peptides to allow cell penetration. TrSOD, TAT-TrSOD-Yfp (fused to yellow fluorescent protein), and Ab-TrSOD were expressed in E. coli and purified as soluble proteins. The cytotoxicity of the enzymes, at the concentrations of 1, 3, and 6 μmol/L, was evaluated for a period of 24 and 48 h of incubation, with no cytotoxic effect on 3T3 fibroblasts. The 3T3 cells were exposed to the oxidant agent tert-butyl hydroperoxide and evaluated for reactive oxygen species (ROS) generation, in the presence or not of the recombinant enzymes. TAT-TrSOD-Yfp was able to decrease the generation of ROS by 15% when used in the concentrations of 3 and 6 μmol/L in comparison to the control, but there was no difference in relation to the effect of TrSOD. Ab-TrSOD, when compared to TrSOD, promoted a decrease in the formation of ROS of 19% and 14% at the concentrations of 1 and 6 μmol/L, respectively, indicating that this recombinant form was more effective in reducing oxidative stress compared to SOD without the cell-penetrating peptide (CPP). Together, these results indicate that the fusion of SOD with these CPP increased the antioxidant capacity of fibroblasts, identified by the reduction in the generation of ROS. In addition, such molecules, in the concentrations initially used, were not toxic to the cells, opening perspectives for the development

show abstract

Section: Resultssupporting

confidence: 92%

Section: Introductionmentioning

confidence: 99%

Delivery of superoxide dismutase by TAT and abalone peptides for the protection of skin cells against oxidative stress

Reigado

Adriani

Santos

et al. 2022

Biotech and App Biochem

View full text Add to dashboard Cite

show abstract

“…Superoxide Dismutase from T. reesei was classified as a MnSOD 88 and is located in mitochondria, playing an important role in the antioxidant defense for the organelle. It has >80% residue identity to other SOD enzymes from filamentous fungi, and a high enzymatic activity (1000 U/mg) compared with other SODs.…”

Section: Manganese-superoxide Dismutase (Mnsod) Of Trichoderma Reeseimentioning

confidence: 99%

“…This enzyme has been broadly studied and is very stable and retains biological activity at temperatures between 20 to 90°C for one hour at pH from 8 to 11.5 making it an ideal model for the Mn/FeSOD family. 88 Each monomer consists of 212 residues and the amino acids specific for MnSOD (M27, G73, G74, H75, Q149 and D150) reported in the previous methods, are shown in the Figure 4 (in the numbering scheme adopted on MnSOD from Trichoderma reesei).…”

Section: Manganese-superoxide Dismutase (Mnsod) Of Trichoderma Reeseimentioning

confidence: 99%

See 1 more Smart Citation

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Rengifo¹

View full text Add to dashboard Cite

With love, to my parents (Genaro and Zenaida) and my brothers (Anibal, Samuel and Genaro) I would like to express my sincerest thanks and appreciation to my adviser, Professor Dr. Richard Garratt, for all his support, and vast knowledge on all things. Whenever I ran into trouble or had a question about the research, his office was always open. His observations and comments helped me to establish the overall direction of the research. I would like to specifically thank Prof. Dr. Jose Ribamar for the fruitful collaboration behind our mutational experiments, and for inspiring my creativity in research. I owe a debt of gratitude to Professor Dr. James Penner-Hahn for giving me the opportunity to work in his lab, for his absolute support of my thesis and for providing me with all the necessary facilities for our research collaboration. I am thankful to Prof. Dr. Pecoraro and Dr. Stuckey for the help and support during my stay in Michigan. I thank Dr. Annirudha and Postdoc Luis Basso for their assistance with the EPR experiments. I extend my gratitude also to Dr. Carol Ann Pitcairn for her care and precious friendship during my stay at the University of Michigan as well as her continued support and friendship thereafter.

show abstract

Fungal biodiversity to biotechnology

Chambergo

Valencia

2016

Appl Microbiol Biotechnol

View full text Add to dashboard Cite

Fungal habitats include soil, water, and extreme environments. With around 100,000 fungus species already described, it is estimated that 5.1 million fungus species exist on our planet, making fungi one of the largest and most diverse kingdoms of eukaryotes. Fungi show remarkable metabolic features due to a sophisticated genomic network and are important for the production of biotechnological compounds that greatly impact our society in many ways. In this review, we present the current state of knowledge on fungal biodiversity, with special emphasis on filamentous fungi and the most recent discoveries in the field of identification and production of biotechnological compounds. More than 250 fungus species have been studied to produce these biotechnological compounds. This review focuses on three of the branches generally accepted in biotechnological applications, which have been identified by a color code: red, green, and white for pharmaceutical, agricultural, and industrial biotechnology, respectively. We also discuss future prospects for the use of filamentous fungi in biotechnology application.

show abstract

Conformational stability of recombinant manganese superoxide dismutase from the filamentous fungus Trichoderma reesei

Cited by 10 publications

References 50 publications

Delivery of superoxide dismutase by TAT and abalone peptides for the protection of skin cells against oxidative stress

Delivery of superoxide dismutase by TAT and abalone peptides for the protection of skin cells against oxidative stress

Exploring the selectivity of metal ions in the active site of the enzyme superoxide dismutase (SOD) using site-directed mutagenesis

Fungal biodiversity to biotechnology

Contact Info

Product

Resources

About