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Chitinases produced by Paenibacillus illinoisensis and Bacillus thuringiensis subsp. pakistani degrade Nod factor from Bradyrhizobium japonicum.

Jung WJ, Mabood F, Souleimanov A, Park RD, Smith DL

Department of Plant Science, McGill University, Macdonald Campus, 21,111 Lakeshore Road, St Anne-de-Bellevue, Que., Canada H9X 3V9.

Chitinases are enzymes that hydrolyze internal beta-1,4-N-acetyl-d-glucosamine linkages of chitin. Since the backbone of Nod factors is a chitin oligomer, we investigated whether chitinases produced by soil bacteria Paenibacillus illinoisensis KJA-424 and Bacillus thuringiensis subsp. Pakistani HD 395 are able to degrade Nod factor produced by Bradyrhizobium japonicum, a phenomenon that could disrupt B. japonicum-soybean signaling and nodule establishment when chitinases are present. Purified Nod factor [LCO Nod Bj-V (C(18:1), MeFuc)] was isolated from Bradyrhizobium japonicum and incubated with crude chitinases isolated from KJA-424 and HD395, with or without acetate buffer. After 15h of incubation, Nod factor in the resulting solution was quantified by HPLC. Degradation was greatest following treatment with KJA-424 (91.9%) and HD395 (86.5%) chitinases in acetate buffer. Treatments that included acetate buffer had higher levels of degradation than those without. For all treatments degradation was greater than 77%.

Published 14 August 2006 in Microbiol Res.
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