2007 journal article
Expression and characterization of Acidothermus cellulolyticus E1 endoglucanase in transgenic duckweed Lemna minor 8627
BIORESOURCE TECHNOLOGY, 98(15), 2866–2872.
author keywords: Acidothermus cellulolyticus; endoglucanase E1; gene expression; Lemna minor; transgenic duckweed
MeSH headings : Buffers; Cellulase / genetics; Cellulase / isolation & purification; Cellulase / metabolism; Gram-Positive Bacteria / enzymology; Hydrogen-Ion Concentration; Plants, Genetically Modified; Temperature
TL;DR:
Duckweed may offer new options for the expression of cellulolytic enzymes in transgenic plants, and the endoglucanase E1 enzyme was biologically active and the expression level was up to 0.24% of total soluble protein.
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Source: Web Of Science
Added: August 6, 2018
Endoglucanase E1 from Acidothermus cellulolyticus was expressed cytosolically under control of the cauliflower mosaic virus 35S promoter in transgenic duckweed, Lemna minor 8627 without any obvious observable phenotypic effects on morphology or rate of growth. The recombinant enzyme co-migrated with the purified catalytic domain fraction of the native E1 protein on western blot analysis, revealing that the cellulose-binding domain was cleaved near or in the linker region. The duckweed-expressed enzyme was biologically active and the expression level was up to 0.24% of total soluble protein. The endoglucanase activity with carboxymethylcellulose averaged 0.2 units mg protein−1 extracted from fresh duckweed. The optimal temperature and pH for E1 enzyme activity were about 80 °C and pH 5, respectively. While extraction with HEPES (N-[2-hydroxyethyl]piperazine-N′-[2-ethanesulfonic acid]) buffer (pH 8) resulted in the highest recovery of total soluble proteins and E1 enzyme, extraction with citrate buffer (pH 4.8) at 65 °C enriched relative amounts of E1 enzyme in the extract. This study demonstrates that duckweed may offer new options for the expression of cellulolytic enzymes in transgenic plants.
