Literature DB >> 20919818

Superoxide dismutase: an industrial perspective.

Amit Bafana1, Som Dutt, Sanjay Kumar, Paramvir S Ahuja.   

Abstract

The application of enzyme technologies to industrial research, development, and manufacturing has become a very important field. Since the production of crude rennet in 1874, several enzymes have been commercialized, and used for therapeutic, supplementary, and other applications. Recent advancements in biotechnology now allow companies to produce safer and less expensive enzymes with enhanced potency and specificity. Antioxidant enzymes are emerging as a new addition to the pool of industrial enzymes and are surpassing all other enzymes in terms of the volume of research and production. In the 1990s, an antioxidant enzyme--superoxide dismutase (SOD)--was introduced into the market. Although the enzyme initially showed great promise in therapeutic applications, it did not perform up to expectations. Consequently, its use was limited to non-drug applications in humans and drug applications in animals. This review summarizes the rise and fall of SOD at the industrial level, the reasons for this, and potential future thrust areas that need to be addressed. The review also focuses on other industrially relevant aspects of SOD such as industrial importance, enzyme engineering, production processes, and process optimization and scale-up.

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Year:  2010        PMID: 20919818     DOI: 10.3109/07388551.2010.490937

Source DB:  PubMed          Journal:  Crit Rev Biotechnol        ISSN: 0738-8551            Impact factor:   8.429


  17 in total

1.  Complete Amino Acid Sequence of a Copper/Zinc-Superoxide Dismutase from Ginger Rhizome.

Authors:  Yuki Nishiyama; Tamo Fukamizo; Kazunari Yoneda; Tomohiro Araki
Journal:  Protein J       Date:  2017-04       Impact factor: 2.371

Review 2.  Simple biological systems for assessing the activity of superoxide dismutase mimics.

Authors:  Artak Tovmasyan; Julio S Reboucas; Ludmil Benov
Journal:  Antioxid Redox Signal       Date:  2013-10-19       Impact factor: 8.401

3.  Identification of host factors limiting the overexpression of recombinant Cu, Zn superoxide dismutase in Escherichia coli.

Authors:  Shweta Guleria; Robin Joshi; Dharam Singh; Sanjay Kumar
Journal:  Biotechnol Lett       Date:  2020-07-10       Impact factor: 2.461

4.  Superoxide dismutase and ascorbate peroxidase are constitutively more thermotolerant than other antioxidant enzymes in Chenopodium album.

Authors:  Renu Khanna-Chopra; Vimal Kumar Semwal
Journal:  Physiol Mol Biol Plants       Date:  2011-09-21

5.  Engineering a thermo-stable superoxide dismutase functional at sub-zero to >50°C, which also tolerates autoclaving.

Authors:  Arun Kumar; Som Dutt; Ganesh Bagler; Paramvir Singh Ahuja; Sanjay Kumar
Journal:  Sci Rep       Date:  2012-04-30       Impact factor: 4.379

6.  Formation of high-order oligomers by a hyperthemostable Fe-superoxide dismutase (tcSOD).

Authors:  Sha Wang; Zhi-Yang Dong; Yong-Bin Yan
Journal:  PLoS One       Date:  2014-10-14       Impact factor: 3.240

7.  A novel mechanism of protein thermostability: a unique N-terminal domain confers heat resistance to Fe/Mn-SODs.

Authors:  Wei Wang; Ting Ma; Baoliang Zhang; Nana Yao; Mingchang Li; Lianlei Cui; Guoqiang Li; Zhenping Ma; Jiansong Cheng
Journal:  Sci Rep       Date:  2014-12-02       Impact factor: 4.379

8.  Characteristics of the Copper,Zinc Superoxide Dismutase of a Hadal Sea Cucumber (Paelopatides sp.) from the Mariana Trench.

Authors:  Yanan Li; Xue Kong; Jiawei Chen; Helu Liu; Haibin Zhang
Journal:  Mar Drugs       Date:  2018-05-18       Impact factor: 5.118

Review 9.  Protein Recovery from Underutilised Marine Bioresources for Product Development with Nutraceutical and Pharmaceutical Bioactivities.

Authors:  Trung T Nguyen; Kirsten Heimann; Wei Zhang
Journal:  Mar Drugs       Date:  2020-07-27       Impact factor: 5.118

10.  Improving the thermostability and stress tolerance of an archaeon hyperthermophilic superoxide dismutase by fusion with a unique N-terminal domain.

Authors:  Mingchang Li; Lin Zhu; Wei Wang
Journal:  Springerplus       Date:  2016-03-01
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