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Oligomerization of Cry9Aa in solution without receptor binding, is not related with insecticidal activity Electron. J. Biotechnol.
Fang,Longfa; Wang,Bo; Zhou,Zishan; Yang,Sujuan; Shu,Changlong; Song,Fuping; Bravo,Alejandra; Soberón,Mario; Zhang,Jie.
Background: Bacillus thuringiensis Cry toxins bind with different insect midgut proteins leading to toxin oligomerization, membrane insertion and pore formation. However, different Cry toxins had been shown to readily form high molecular weight oligomers or aggregates in solution in the absence of receptor interaction. The role of Cry oligomers formed in solution remains uncertain. The Cry9A proteins show high toxicity against different Lepidoptera, and no-cross resistance with Cry1A. Results: Cry9Aa655 protein formed oligomers easily in solution mediated by disulfide bonds, according to SDS-PAGE analysis under non-reducing and reducing conditions. However, oligomerization is not observed if Cry9Aa655 is activated with trypsin, suggesting that cysteine...
Tipo: Journal article Palavras-chave: Cry9Aa655; Disulfide bonds; Oligomerization; Insecticidal activity.
Ano: 2016 URL: http://www.scielo.cl/scielo.php?script=sci_arttext&pid=S0717-34582016000300006
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Screening and characterization of a novel alkaline lipase from Acinetobacter calcoaceticus 1-7 isolated from Bohai Bay in China for detergent formulation BJM
Wang,Haikuan; Zhong,Shaojiong; Ma,Huijing; Zhang,Jie; Qi,Wei.
A novel alkaline lipase-producing strain 1-7 identified as Acinetobacter calcoaceticus was isolated from soil samples collected from Bohai Bay, China, using an olive oil alkaline plate, which contained olive oil as the sole carbon source. The lipase from strain 1-7 showed the maximum activity at pH 9.0 under 40ºC. One interesting feature of this enzyme is that it exhibits lipase activity over a broad range of temperatures and good stability. It is also stable at a broad range of pHs from 4.0 to 10.0 for 24 h. Its catalytic activity was highly enhanced in the presence of Ca2+, Mg2+ and K+, but partially inhibited by Cu2+, Al3+, Fe3+ , Ba2+and Zn2+. The fact that it displays marked stability and activity in the presence of TritonX-100, Tween-20, Tween-80,...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Alkaline lipase; Acinetobacter calcoaceticus; Characterization; Detergent.
Ano: 2012 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822012000100016
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