PMID- 34150734
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20210622
IS  - 2296-4185 (Print)
IS  - 2296-4185 (Electronic)
IS  - 2296-4185 (Linking)
VI  - 9
DP  - 2021
TI  - Production of Glucose 6-Phosphate From a Cellulosic Feedstock in a One Pot 
      Multi-Enzyme Synthesis.
PG  - 678038
LID - 10.3389/fbioe.2021.678038 [doi]
LID - 678038
AB  - Glucose 6-phosphate is the phosphorylated form of glucose and is used as a 
      reagent in enzymatic assays. Current production occurs via a multi-step chemical 
      synthesis. In this study we established a fully enzymatic route for the synthesis 
      of glucose 6-phosphate from cellulose. As the enzymatic phosphorylation requires 
      ATP as phosphoryl donor, the use of a cofactor regeneration system is required. 
      We evaluated Escherichia coli glucokinase and Saccharomyces cerevisiae hexokinase 
      (HK) for the phosphorylation reaction and Pseudomonas aeruginosa polyphosphate 
      kinase 2 (PPK2) for ATP regeneration. All three enzymes were characterized in 
      terms of temperature and pH optimum and the effects of substrates and products 
      concentrations on enzymatic activities. After optimization of the conditions, we 
      achieved a 85% conversion of glucose into glucose 6-phosphate using the HK/PPK2 
      activities within a 24 h reaction resulting in 12.56 g/l of glucose 6-phosphate. 
      Finally, we demonstrated the glucose 6-phosphate formation from microcrystalline 
      cellulose in a one-pot reaction comprising Aspergillus niger cellulase for 
      glucose release and HK/PPK2 activities. We achieved a 77% conversion of released 
      glucose into glucose 6-phosphate, however at the expense of a lower glucose 
      6-phosphate yield of 1.17 g/l. Overall, our study shows an alternative approach 
      for synthesis of glucose 6-phosphate that can be used to valorize biomass derived 
      cellulose.
CI  - Copyright (c) 2021 Usvalampi, Li and Frey.
FAU - Usvalampi, Anne
AU  - Usvalampi A
AD  - Department of Bioproducts and Biosystems, School of Chemical Engineering, Aalto 
      University, Espoo, Finland.
FAU - Li, He
AU  - Li H
AD  - Department of Bioproducts and Biosystems, School of Chemical Engineering, Aalto 
      University, Espoo, Finland.
FAU - Frey, Alexander D
AU  - Frey AD
AD  - Department of Bioproducts and Biosystems, School of Chemical Engineering, Aalto 
      University, Espoo, Finland.
LA  - eng
PT  - Journal Article
DEP - 20210602
PL  - Switzerland
TA  - Front Bioeng Biotechnol
JT  - Frontiers in bioengineering and biotechnology
JID - 101632513
PMC - PMC8206812
OTO - NOTNLM
OT  - ATP regeneration
OT  - Pseudomonas aeruginosa polyphosphate kinase 2
OT  - Saccharomyces cerevisiae hexokinase
OT  - cellulose valorization
OT  - enzymatic phosphorylation
OT  - glucose 6-phosphate
COIS- The authors declare that the research was conducted in the absence of any 
      commercial or financial relationships that could be construed as a potential 
      conflict of interest.
EDAT- 2021/06/22 06:00
MHDA- 2021/06/22 06:01
PMCR- 2021/01/01
CRDT- 2021/06/21 06:00
PHST- 2021/03/08 00:00 [received]
PHST- 2021/05/07 00:00 [accepted]
PHST- 2021/06/21 06:00 [entrez]
PHST- 2021/06/22 06:00 [pubmed]
PHST- 2021/06/22 06:01 [medline]
PHST- 2021/01/01 00:00 [pmc-release]
AID - 10.3389/fbioe.2021.678038 [doi]
PST - epublish
SO  - Front Bioeng Biotechnol. 2021 Jun 2;9:678038. doi: 10.3389/fbioe.2021.678038. 
      eCollection 2021.