PMID- 35025256
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20220113
IS  - 2576-6422 (Electronic)
IS  - 2576-6422 (Linking)
VI  - 3
IP  - 6
DP  - 2020 Jun 15
TI  - Elucidating the Mechanism behind the Bionanomanufacturing of Gold Nanoparticles 
      Using Bacillus subtilis.
PG  - 3859-3867
LID - 10.1021/acsabm.0c00420 [doi]
AB  - Over the last two decades, gold nanoparticles (GNPs) have opened up numerous 
      research and industrial opportunities in biomedical, optical, and electronic 
      fields due to their size- and morphology-dependent properties [Grassian, V. H. 
      Macromolecules 2008, 112(47), 18303-18313 and Nehl, C. L.; Hafner, J. H. J. 
      Mater. Chem. 2008, 18(21), 2415-2419]. Therefore, green and efficient synthesis 
      strategies providing precise control over size and morphology are desired. Since 
      biological catalysts are known for the selectivity, efficiency, and 
      environmentally friendly production of gold nanoparticles (referred to as 
      bionanomanufacturing), they have been considered for GNP synthesis. However, the 
      mechanism of how most of these biological entities produce GNPs has not been 
      elucidated to date, limiting the industrial implementation of complex biological 
      systems for nanoparticle synthesis. In this study, we investigated the mechanism 
      of extracellular GNP production by Bacillus subtilis (B. subtilis). It is shown 
      that B. subtilis releases vegetative catalase (Cat A) into the supernatant. Cat A 
      from the supernatant and commercial catalase were employed to establish the 
      mechanism of GNP formation. The bionanomanufactured GNPs were characterized using 
      ultraviolet-visible (UV-vis) spectroscopy, transmission electron microscopy 
      (TEM), and dynamic light scattering (DLS). Based on our results, we theorize that 
      the mechanism of extracellular GNP production by B. subtilis Cat A involves (1) 
      formation of gold-thiol bonds followed by (2) stabilization of GNPs with the 
      denatured bacterial protein that serves as a capping agent. This research offers 
      early insights into the gold-reducing mechanism occurring in the cell-free 
      extract of B. subtilis, which can potentially lead to the design of protocols for 
      the controlled production of GNPs with isolated enzymes at the industrial scale.
FAU - Lim, Koun
AU  - Lim K
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
FAU - Macazo, Florika C
AU  - Macazo FC
AUID- ORCID: 0000-0001-6706-2407
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
FAU - Scholes, Connor
AU  - Scholes C
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
FAU - Chen, Hui
AU  - Chen H
AUID- ORCID: 0000-0002-8944-0090
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
FAU - Sumampong, Kirsten
AU  - Sumampong K
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
FAU - Minteer, Shelley D
AU  - Minteer SD
AUID- ORCID: 0000-0002-5788-2249
AD  - Department of Chemistry, University of Utah, 315 South 1400 East, RM 2020, Salt 
      Lake City, Utah84112, United States.
LA  - eng
PT  - Journal Article
DEP - 20200604
PL  - United States
TA  - ACS Appl Bio Mater
JT  - ACS applied bio materials
JID - 101729147
SB  - IM
OTO - NOTNLM
OT  - bionanomanufacturing
OT  - catalase
OT  - gold nanoparticles
OT  - gold-thiol bonds
OT  - green synthesis
EDAT- 2020/06/15 00:00
MHDA- 2020/06/15 00:01
CRDT- 2022/01/13 17:13
PHST- 2022/01/13 17:13 [entrez]
PHST- 2020/06/15 00:00 [pubmed]
PHST- 2020/06/15 00:01 [medline]
AID - 10.1021/acsabm.0c00420 [doi]
PST - ppublish
SO  - ACS Appl Bio Mater. 2020 Jun 15;3(6):3859-3867. doi: 10.1021/acsabm.0c00420. Epub 
      2020 Jun 4.