Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions

Linbo Sun; Di Huang; Lin Zhu; Bingling Zhang; Chenchen Peng; Ting Ma; Xin Deng; Junli Wu; Wei Wang

doi:10.1016/j.biortech.2019.01.045

Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions

Linbo Sun
, Di Huang
, Lin Zhu
, Bingling Zhang
, Chenchen Peng
, Ting Ma
, Xin Deng
, Junli Wu
, Wei Wang^*

^*Corresponding author for this work

Department of Biomedical Sciences

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

16 Citations (Scopus)

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.
© 2019 Elsevier Ltd.

Original language	English
Pages (from-to)	73-81
Journal	Bioresource Technology
Volume	278
Online published	11 Jan 2019
DOIs	https://doi.org/10.1016/j.biortech.2019.01.045
Publication status	Published - Apr 2019

Research Keywords

Anaerobic biodegradation
Geobacillus thermoglucosidasius
Nitroalkane compounds
Thermophilic bacterium
Thermophilic enzymes

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title = "Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions",

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. {\textcopyright} 2019 Elsevier Ltd.",

keywords = "Anaerobic biodegradation, Geobacillus thermoglucosidasius, Nitroalkane compounds, Thermophilic bacterium, Thermophilic enzymes",

author = "Linbo Sun and Di Huang and Lin Zhu and Bingling Zhang and Chenchen Peng and Ting Ma and Xin Deng and Junli Wu and Wei Wang",

year = "2019",

month = apr,

doi = "10.1016/j.biortech.2019.01.045",

language = "English",

volume = "278",

pages = "73--81",

journal = "Bioresource Technology",

issn = "0960-8524",

publisher = "Elsevier Ltd.",

}

TY - JOUR

T1 - Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions

AU - Sun, Linbo

AU - Huang, Di

AU - Zhu, Lin

AU - Zhang, Bingling

AU - Peng, Chenchen

AU - Ma, Ting

AU - Deng, Xin

AU - Wu, Junli

AU - Wang, Wei

PY - 2019/4

Y1 - 2019/4

N2 - 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. © 2019 Elsevier Ltd.

AB - 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. © 2019 Elsevier Ltd.

KW - Anaerobic biodegradation

KW - Geobacillus thermoglucosidasius

KW - Nitroalkane compounds

KW - Thermophilic bacterium

KW - Thermophilic enzymes

UR - https://www.scopus.com/pages/publications/85060312382

UR - https://www.scopus.com/record/pubmetrics.uri?eid=2-s2.0-85060312382&origin=recordpage

U2 - 10.1016/j.biortech.2019.01.045

DO - 10.1016/j.biortech.2019.01.045

M3 - RGC 21 - Publication in refereed journal

SN - 0960-8524

VL - 278

SP - 73

EP - 81

JO - Bioresource Technology

JF - Bioresource Technology

ER -

Novel thermostable enzymes from Geobacillus thermoglucosidasius W-2 for high-efficient nitroalkane removal under aerobic and anaerobic conditions

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Research Keywords

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