Expression and biochemical characterization of a novel type I pullulanase from Bacillus megaterium

2016 ◽  
Vol 39 (3) ◽  
pp. 397-405 ◽  
Author(s):  
Shaoqing Yang ◽  
Qiaojuan Yan ◽  
Qingdan Bao ◽  
Jingjing Liu ◽  
Zhengqiang Jiang
2015 ◽  
Vol 77 ◽  
pp. 527-533 ◽  
Author(s):  
Sunyan Zhang ◽  
Yajuan Xie ◽  
Chong Zhang ◽  
Xiaomei Bie ◽  
Haizhen Zhao ◽  
...  

1996 ◽  
Vol 138 (2-3) ◽  
pp. 147-152 ◽  
Author(s):  
Cheorl-Ho Kim ◽  
Oyekanmi Nashiru ◽  
Jeong Heon Ko

2011 ◽  
Vol 48 (3) ◽  
pp. 260-266 ◽  
Author(s):  
Jinho Kang ◽  
Kyung-Min Park ◽  
Kyoung-Hwa Choi ◽  
Cheon-Seok Park ◽  
Go-Eun Kim ◽  
...  

2016 ◽  
Vol 473 (10) ◽  
pp. 1443-1453 ◽  
Author(s):  
Louis Carles ◽  
Pascale Besse-Hoggan ◽  
Muriel Joly ◽  
Armelle Vigouroux ◽  
Solange Moréra ◽  
...  

Mesotrione is a selective herbicide belonging to the triketone family, commonly used on maize cultures since 2003. A mesotrione-transforming Bacillus megaterium Mes11 strain isolated from an agricultural soil was used as a model to identify the key enzymes initiating the biotransformation of this herbicide. Two enzymes (called NfrA1 and NfrA2/YcnD) were identified, and functionally and structurally characterized. Both belong to the NfsA FRP family of the nitro-FMN reductase superfamily (type I oxygen-insensitive nitroreductase) and show optimal pH and temperature of 6–6.5 and 23–25°C, respectively. Both undergo a Ping Pong Bi Bi mechanism, with NADPH and NADPH/NADH as cofactors for NfrA1 and NfrA2/YcnD, respectively. It is interesting that both can also reduce various nitro compounds including pesticides, antibiotics, one prodrug and 4-methylsulfonyl-2-nitrobenzoic acid, one of the mesotrione metabolites retrieved from the environment. The present study constitutes the first identification of mesotrione-transforming enzymes. These enzymes (or their corresponding genes) could be used as biomarkers to predict the capacity of ecosystems to transform mesotrione and assess their contamination by both the parent molecule and/or the metabolites.


2018 ◽  
Vol 70 (5-6) ◽  
pp. 1700179 ◽  
Author(s):  
Lingmeng Li ◽  
Fengying Dong ◽  
Lin Lin ◽  
Dannong He ◽  
Jingwen Chen ◽  
...  

2005 ◽  
Vol 70 (3) ◽  
pp. 347-360 ◽  
Author(s):  
Tanja Cirkovic-Velickovic ◽  
Marija Gavrovic-Jankulovic ◽  
Ratko Jankov

The characterization of an allergen is a troublesome and difficult process, as it requires both the precise biochemical characterization of a (glyco)protein molecule and the establishment of its susceptibility to IgE antibodies, as they are the main link to histamine release in some hypersensitivity states (type I allergies). As the characterization of an allergen includes molecular weight determination of the allergenic molecule, its structure determination, physicochemical properties, IgE binding properties of the allergen molecule, and its allergenicity, an overall review of which biochemical and immunochemical methods are used in achieving this goal are presented in this paper. The information on the molecular level on the structures of allergens indicates that allergens are considerably heterogeneous protein structures, and that there is no particular aminoacid sequence which is responsible for the allergenicity. Therefore, information gained from detailed structural, functional and immunochemical studies of these intriguing molecules, which nowadays modulate a variety of pathophysiological conditions, would greatly improve our understanding of the underlying disease mechanisms, and the way to handle them.


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