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Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica

Paper ID Volume ID Publish Year Pages File Format Full-Text
35332 45087 2009 6 PDF Available
Title
Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica
Abstract

Superoxide dismutase (SOD) catalyzes the conversion of the superoxide radical (O2−) into oxygen and hydrogen peroxide. Deschampsia antarctica is a plant that grows in Antarctica and survives to extreme low temperature and high UV radiation, thus it is an ideal model to study novel antioxidants. A cDNA Cu/Zn-SOD gene from D. antarctica was cloned into a pET vector and expressed in Escherichia coli BL21-SI. 112 mg/L of recombinant Cu/Zn-SOD was attained in batch cultures in bioreactor. Using Ni-affinity gel chromatography, the recombinant Cu/Zn-SOD was recovered with a purity of 90% and a specific enzyme activity of 749 at 25 °C. However, zymogram test showed that the enzyme has more activity at 4 °C. This D. antarctica SOD could be used to reduce the oxidation of refrigerated and frozen foods.

Keywords
Antioxidant; Plant; Extremophil; Psychrophilic enzyme; Photo-oxidation; Oxidative stress
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Heterologous expression of a novel psychrophilic Cu/Zn superoxide dismutase from Deschampsia antarctica
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Publisher
Database: Elsevier - ScienceDirect
Journal: Process Biochemistry - Volume 44, Issue 9, September 2009, Pages 969–974
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us