Abstract

An inexpensive source of industrially useful enzymes is critical for their commercial production. We have produced an industrially valuable recombinant superoxide dismutase (SOD) in tobacco chloroplasts. A gene from Withania somnifera, encoding a highly stable Cu/Zn SOD, was cloned into a chloroplast transformation vector. It expressed the SOD in tobacco chloroplasts following transformation. The transplastomic plants accumulated the recombinant SOD at up to ∼9 % of the total soluble protein in leaves. The purified chloroplast-expressed recombinant SOD had an estimated specific activity of ∼4600 U/mg. Like the native enzyme, purified recombinant enzyme, prepared from tobacco leaves, was highly stable at high temperatures and tolerated a wide pH range, SDS, ethanol and protease treatment. The results establish the potential of chloroplast transformation for commercial production of recombinant SOD in plants.

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