학술논문
Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions.
Document Type
Article
Author
Source
Subject
*THERMOPHILIC bacteria
*NITROALKANES
*ANAEROBIC digestion
*NITROPROPANE
*BACTERIAL enzymes
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Language
ISSN
0960-8524
Abstract
Graphical abstract Highlights • Thermophile W-2 could degrade nitroalkane under aerobic and anaerobic conditions. • Three NOEs displayed high optimum active temperature and wide substrate specificity. • Gt2929 possessed excellent specific activity, thermostability and pH stability. • Gt1378 played an important role in anaerobic degradation. Abstract In this study, a thermophilic facultative anaerobic strain Geobacillus thermoglucosidasius W-2 was found to degrade nitroalkane under both aerobic and anaerobic conditions. Bioinformatical analysis revealed three putative nitroalkane-oxidizing enzymes (Gt-NOEs) genes from the W-2 genome. The three identified proteins Gt2929, Gt1378, and Gt1208 displayed optimal activities at high temperatures (70, 70, and 80 °C, respectively). Among these, Gt2929 exhibited excellent degradation capability, pH stability, and metal ion tolerance for nitronates under aerobic condition. Interestingly, under anaerobic condition, only Gt1378 still maintained high activity for 2-nitropropane and nitroethane, indicating that the W-2 strain utilized various pathways to degrade nitronates under aerobic and anaerobic conditions, respectively. Taken together, the first revelation of thermophilic nitroalkane-degrading mechanism under both aerobic and anaerobic conditions provides guidance and platform for biotechnological and industrial applications. [ABSTRACT FROM AUTHOR]