The gene encoding an extracellular isomalto-dextranase, designated imd, was isolated from the chromosomal DNA of Arthrobacter globiformis T6 and cloned and expressed in Escherichia coli. A single open reading frame consisting of 1,926 base pairs that encoded a polypeptide composed of a signal peptide of 39 amino acids and a mature protein of 602 amino acids (M(r), 65,900) was found. The primary structure had no significant homology with the structures of any other reported carbohydrases, including two other dextranases. Transformed E. coli cells carrying the 2.3-kb fragment overproduced isomalto-dextranase into the periplasmic space under control of the promoter of the imd gene itself.
References
https://doi.org/10.1128/jb.176.24.7730-7734.1994
https://www.researchgate.net/publication/15195843_Molecular_cloning_andexpression_of_an_isomalto-dextranase_gene_from_Anhrobacter_globiformis_T6
This 1994 molecular biology study focused on enzymatic polysaccharide metabolism in Arthrobacter globiformis, contributing to understanding carbohydrate-active enzymes.
An isomalto-dextranase gene from Arthrobacter globiformis T6 was cloned and expressed. This enzyme catalyzes hydrolysis of dextran, revealing how bacteria process complex polysaccharides at the molecular level.
While not studying beta glucans directly, polysaccharide-degrading enzyme research provides foundational knowledge about microbial carbohydrate metabolism relevant to glucan biosynthesis in organisms like Aureobasidium pullulans.
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Iwai A., Ito H., Mizuno T., Mori H., Matsui H.. Molecular cloning and expression of an isomalto-dextranase gene from Arthrobacter globiformis T6. Journal of Bacteriology. 1994. DOI: 10.1128/jb.176.24.7730-7734.1994.
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