Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2020 Aug 20;10(51):30953-30960.
doi: 10.1039/d0ra03160g. eCollection 2020 Aug 17.

Organic-inorganic nanocrystal reductase to promote green asymmetric synthesis

Kotchakorn T Sriwong  1 , Afifa Ayu Koesoema  1 , Tomoko Matsuda  1
Affiliations

Organic-inorganic nanocrystal reductase to promote green asymmetric synthesis

Kotchakorn T Sriwong et al. RSC Adv. .

Abstract

An acetophenone reductase from Geotrichum candidum (GcAPRD) was immobilized by the organic-inorganic nanocrystal method. The GcAPRD nanocrystal presented improved stability and recyclability compared with those of the free GcAPRD. Moreover, the GcAPRD nanocrystal reduced broad kinds of ketones with excellent enantioselectivities to produce beneficial chiral alcohols such as (S)-1-(3',4'-dichlorophenyl)ethanol with >99% yield and >99% ee. The robust and versatile properties of the GcAPRD nanocrystal demonstrated an approach to promote green asymmetric synthesis and sustainable chemistry.

PubMed Disclaimer

Conflict of interest statement

There are no conflicts to declare.

Figures

Fig. 1
Fig. 1. Optimization of GcAPRD nanocrystal preparation (a) metal ions, (b) metal ion (Co2+) concentration, (c) PBS concentration, (d) PBS pH, and (e) protein concentration. Left and right column depict the immobilization yields and relative reaction yields, respectively. The reaction yield of free GcAPRD was set to be 100%. *Very small precipitation was found. The preparation and reaction conditions are described in the section 2.4.
Fig. 2
Fig. 2. SEM images of GcAPRD nanocrystal formed under various protein concentrations, (a and b) control (no enzyme), (c and d) 0.02 mg mL−1, (e and f) 0.10 mg mL−1, (g and h) 0.50 mg mL−1, and (i and j) 2.00 mg mL−1.
Fig. 3
Fig. 3. The proposed formation mechanism of GcAPRD nanocrystal, comprised of 3 steps: (1) nucleation, (2) aggregation, and (3) anisotropic growth.
Fig. 4
Fig. 4. Temperature and pH profile, and stability of free GcAPRD (orange-circle line) and GcAPRD nanocrystal (blue-square line). (a) temperature profile, (b) pH profile, and (c) storage stability. Enzyme activities of free GcAPRD and GcAPRD nanocrystal at 37 °C for (a), HEPES–NaOH buffer (pH 7.0) for (b), and day 0 for (c) were set to be 100%. For the pH profile, the enzyme activity was measured in MES–NaOH buffer (0.10 M) (dotted line), HEPES–NaOH buffer (0.10 M) (line), and glycine–NaOH buffer (0.10 M) (broken line). The activity assay is described in the section 2.4.
Fig. 5
Fig. 5. Recyclability of GcAPRD nanocrystal. The reaction condition is described in the section 2.4.
See this image and copyright information in PMC

References

    1. Nakamura K. Yamanaka R. Matsuda T. Harada T. Tetrahedron: Asymmetry. 2003;14:2659–2681. doi: 10.1016/S0957-4166(03)00526-3. - DOI
    1. Madhavan A. Sindhu R. Binod P. Sukumaran R. K. Pandey A. Bioresour. Technol. 2017;245:1304–1313. doi: 10.1016/j.biortech.2017.05.031. - DOI - PubMed
    1. Stampfer W. Kosjek B. Faber K. Kroutil W. J. Org. Chem. 2003;68:402–406. doi: 10.1021/jo026216w. - DOI - PubMed
    1. Giersberg M. Degelmann A. Bode R. Piontek M. Kunze G. J. Ind. Microbiol. Biotechnol. 2012;39:1385–1396. doi: 10.1007/s10295-012-1134-9. - DOI - PubMed
    1. Choi J.-M. Han S.-S. Kim H.-S. Biotechnol. Adv. 2015;33:1443–1454. doi: 10.1016/j.biotechadv.2015.02.014. - DOI - PubMed