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 signalling 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 15 h 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%. (c)(c) 2006 Published by Elsevier GmbH.
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Karadeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, Turkey
Giresun Univ, Fac Arts & Sci, Dept Biol, Giresun, TurkeyKaradeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, Turkey
Ugras, Serpil
Sezen, Kazim
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Karadeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, TurkeyKaradeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, Turkey
Sezen, Kazim
Kati, Hatice
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Giresun Univ, Fac Arts & Sci, Dept Biol, Giresun, TurkeyKaradeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, Turkey
Kati, Hatice
Demirbag, Zihni
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Karadeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, TurkeyKaradeniz Tech Univ, Fac Sci, Dept Biol, Trabzon, Turkey