PMID- 28587256
OWN - NLM
STAT- MEDLINE
DCOM- 20180326
LR  - 20181113
IS  - 1422-0067 (Electronic)
IS  - 1422-0067 (Linking)
VI  - 18
IP  - 6
DP  - 2017 Jun 5
TI  - Biochemical and Computational Insights on a Novel Acid-Resistant and 
      Thermal-Stable Glucose 1-Dehydrogenase.
LID - 10.3390/ijms18061198 [doi]
LID - 1198
AB  - Due to the dual cofactor specificity, glucose 1-dehydrogenase (GDH) has been 
      considered as a promising alternative for coenzyme regeneration in biocatalysis. 
      To mine for potential GDHs for practical applications, several genes encoding for 
      GDH had been heterogeneously expressed in Escherichia coli BL21 (DE3) for primary 
      screening. Of all the candidates, GDH from Bacillus sp. ZJ (BzGDH) was one of the 
      most robust enzymes. BzGDH was then purified to homogeneity by immobilized metal 
      affinity chromatography and characterized biochemically. It displayed maximum 
      activity at 45  degrees C and pH 9.0, and was stable at temperatures below 50  degrees C. BzGDH 
      also exhibited a broad pH stability, especially in the acidic region, which could 
      maintain around 80% of its initial activity at the pH range of 4.0-8.5 after 
      incubating for 1 hour. Molecular dynamics simulation was conducted for better 
      understanding the stability feature of BzGDH against the structural context. The 
      in-silico simulation shows that BzGDH is stable and can maintain its overall 
      structure against heat during the simulation at 323 K, which is consistent with 
      the biochemical studies. In brief, the robust stability of BzGDH made it an 
      attractive participant for cofactor regeneration on practical applications, 
      especially for the catalysis implemented in acidic pH and high temperature.
FAU - Ding, Haitao
AU  - Ding H
AD  - Key Laboratory for Polar Science of State Oceanic Administration, Polar Research 
      Institute of China, Shanghai 200136, China. dinghaitao@pric.org.cn.
FAU - Gao, Fen
AU  - Gao F
AD  - East China Sea Fisheries Research Institute, Shanghai 200090, China. 
      gaofen2011@163.com.
FAU - Yu, Yong
AU  - Yu Y
AD  - Key Laboratory for Polar Science of State Oceanic Administration, Polar Research 
      Institute of China, Shanghai 200136, China. yuyong@pric.org.cn.
FAU - Chen, Bo
AU  - Chen B
AD  - Key Laboratory for Polar Science of State Oceanic Administration, Polar Research 
      Institute of China, Shanghai 200136, China. chenbo@pric.org.cn.
LA  - eng
PT  - Journal Article
DEP - 20170605
PL  - Switzerland
TA  - Int J Mol Sci
JT  - International journal of molecular sciences
JID - 101092791
RN  - 0 (Recombinant Proteins)
RN  - EC 1.1.1.47 (Glucose 1-Dehydrogenase)
SB  - IM
MH  - Amino Acid Motifs
MH  - Amino Acid Sequence
MH  - Bacillus/enzymology
MH  - Biocatalysis
MH  - Conserved Sequence
MH  - Enzyme Stability
MH  - Glucose 1-Dehydrogenase/*chemistry/genetics/metabolism
MH  - *Hydrogen-Ion Concentration
MH  - Kinetics
MH  - *Models, Molecular
MH  - Phylogeny
MH  - Protein Conformation
MH  - Recombinant Proteins/chemistry/genetics/metabolism
MH  - Structure-Activity Relationship
MH  - Substrate Specificity
MH  - Temperature
PMC - PMC5486021
OTO - NOTNLM
OT  - Bacillus
OT  - acid-resistant
OT  - glucose 1-dehydrogenase
OT  - molecular dynamics simulation
OT  - thermal-stable
COIS- The authors declare no conflict of interest.
EDAT- 2017/06/08 06:00
MHDA- 2018/03/27 06:00
PMCR- 2017/06/01
CRDT- 2017/06/08 06:00
PHST- 2017/05/10 00:00 [received]
PHST- 2017/05/30 00:00 [revised]
PHST- 2017/05/30 00:00 [accepted]
PHST- 2017/06/08 06:00 [entrez]
PHST- 2017/06/08 06:00 [pubmed]
PHST- 2018/03/27 06:00 [medline]
PHST- 2017/06/01 00:00 [pmc-release]
AID - ijms18061198 [pii]
AID - ijms-18-01198 [pii]
AID - 10.3390/ijms18061198 [doi]
PST - epublish
SO  - Int J Mol Sci. 2017 Jun 5;18(6):1198. doi: 10.3390/ijms18061198.