Biomanufacturing of CdS quantum dots

Zhou, Yang; Li, Lu; Berard, Victoria F.; He, Qian; Kiely, Christopher J.; Berger, Bryan W.; McIntosh, Steven

doi:10.1039/c5gc00194c

Cited by 76 publications

(84 citation statements)

References 51 publications

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“…For reference, our previous work (32) demonstrated that absorption peak maxima of 324, 334, and 344 nm correspond to biomineralized nanocrystallite sizes of 2.75 ± 0.68, 3.04 ± 0.75, and 3.36 ± 0.95 nm, respectively. Additionally, smCSEproduced CdS nanocrystals show similar quantum yield (1.8%) compared with synthesized CdS nanocrystals from S. maltophilia (2%) (32).…”

Section: Enzymatically Synthesized Cds Quantum Dots Are Monodisperse mentioning

confidence: 74%

“…We previously identified a putative cystathionine γ-lyase (smCSE) associated with the extracellular synthesis of CdS quantum dot nanocrystals by Stenotrophomonas maltophilia strain SMCD1 (32). Cystathionine γ-lyases (CSEs) are a class of enzymes that catalyze the production of H 2 S, NH 3 and pyruvate from L-cysteine, and the overexpression of which has been shown to precipitate cadmium sulfide (33).…”

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confidence: 99%

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Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties

Dunleavy

Kiely

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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115

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Nature has evolved several unique biomineralization strategies to direct the synthesis and growth of inorganic materials. These natural systems are complex, involving the interaction of multiple biomolecules to catalyze biomineralization and template growth. Herein we describe the first report to our knowledge of a single enzyme capable of both catalyzing mineralization in otherwise unreactive solution and of templating nanocrystal growth. A recombinant putative cystathionine γ-lyase (smCSE) mineralizes CdS from an aqueous cadmium acetate solution via reactive H 2 S generation from L-cysteine and controls nanocrystal growth within the quantum confined size range. The role of enzymatic nanocrystal templating is demonstrated by substituting reactive Na 2 S as the sulfur source. Whereas bulk CdS is formed in the absence of the enzyme or other capping agents, nanocrystal formation is observed when smCSE is present to control the growth. This dualfunction, single-enzyme, aerobic, and aqueous route to functional material synthesis demonstrates the powerful potential of engineered functional material biomineralization.cadmium sulfide | quantum dot | biomineralization | enzyme | nanoparticle B iological systems have evolved a diverse array of mechanisms to synthesize inorganic materials from aqueous solutions under ambient conditions. This inherent control over material properties has created interest in using these biological routes to synthesize materials (1-3) such as biosilica from sponges and diatoms (4-8), biogenic CaCO 3 from mollusks (9-12), and magnetic particles from magnetotactic bacteria (13-15). Designing a biomineralization strategy requires control of both the material composition and structure; in nature, this control is typically achieved through the assembly of a multiprotein complex, including both structuredirecting proteins and proteins responsible for mineralization of a specific composition. In the current work, we demonstrate the reduction of this complexity to its simplest form: a single enzyme capable of both catalyzing CdS mineralization and controlling particle size within the quantum confined size range to form functional biomineralized CdS quantum dots.Two of the most studied biomineralization proteins are perlucin and silicatein. Perlucin (16) has been shown to mineralize crystalline forms of CaCO 3 , a common structural material that constitutes the shell of many marine organisms, in the form of organic-inorganic composites. The role of the nacre protein perlucin in crystallite templating has been elucidated through experiments demonstrating crystallite formation in the presence of purified perlucin, and perlucin selectively being removed from solution during crystallite formation in the presence of a mixture of water-soluble, nacre-associated proteins (17). Native silicatein harvested from sea sponge or engineered forms produced recombinantly are active for biomineralization of silica and titania into structures that are amorphous or crystalline (7,18,19). In particular, biomineralizatio...

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Section: Enzymatically Synthesized Cds Quantum Dots Are Monodisperse mentioning

confidence: 74%

mentioning

confidence: 99%

Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties

Dunleavy

Kiely

et al. 2016

Proc. Natl. Acad. Sci. U.S.A.

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115

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“…[14] It should be noted that extracellular production is preferable as it eliminates the requirement for cell lysis during harvesting, decreasing protein and other biomacromolecule contamination of the obtained nanocrystals. [24] However, the exact extracellular mechanism of CdS formation still remains unclear and requires further detailed investigation.…”

Section: Comparative Analysismentioning

confidence: 99%

“…[23] Formation of 3 § 0.2 nm-sized CdS nanoparticles was determined by HRTEM measurements. [24] In another study, [15] formation of extracellular CdS nanoparticles (5À20 nm in size) was achieved by the enzymatic reduction of sulphate ions by Fusarium biomass. Compared to our previous studies, [12,13] it could be concluded that all tested matrices (bacteria, plant culture and fungal mycelium) can be considered effective for extracellular, eco-friendly biosynthesis of CdS nanoparticles.…”

Section: Comparative Analysismentioning

confidence: 99%

Biosynthesis of cadmium sulphide quantum dots by usingPleurotus ostreatus(Jacq.) P. Kumm

Borovaya

Pirko

Krupodorova

et al. 2015

Biotechnology & Biotechnological Equipment

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The development of 'green' technologies in nanoparticle synthesis is of considerable importance to broaden their biological applications. Cadmium sulphide nanoparticles are considered very promising in applied chemistry, bioscience and medicine. The aim of this study was to develop an efficient, easily reproducible and environmentally friendly method for biosynthesis of cadmium sulphide quantum dots based on the usage of mycelium of the basidiomycete fungus Pleurotus ostreatus. By incubating P. ostreatus mycelium with inorganic cadmium sulphate and sodium sulphide, we synthesized stable luminescent CdS nanocrystals. They showed absorption peaks at 453 nm (ultravioletÀvisible spectrometry) and a main luminescent peak at 462 nm. Transmission electron microscopy revealed that the obtained quantum dots were of a spherical shape and predominantly from 4 to 5 nm in size. The electron diffraction pattern confirmed the wurtzite crystalline structure of the synthesized cadmium sulphide quantum dots. The obtained results confirm for the first time that the system based on basiodiomycete fungi could be considered promising for synthesizing semiconductor quantum dots.

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“…12,13,15,20 Through identification and engineering of a cystathionine γ-lyase (smCSE) enzyme found associated with these nanocrystals, this procedure was simplified to a single enzyme approach for CdS biomineraliza-tion wherein we demonstrated that a single recombinant enzyme acts to both generate reactive sulfur via reduction of L-cysteine and template the formation of size controlled crystalline quantum dots. 20 This class of enzymes catalyze the formation of pyruvate, ammonia, and hydrogen sulfide from L-cysteine, providing the reactive sulfur precursor necessary for biomineralization.…”

Section: ■ Introductionmentioning

confidence: 99%

Single Enzyme Direct Biomineralization of CdSe and CdSe-CdS Core-Shell Quantum Dots

Zhou

Kiely

et al. 2017

ACS Appl. Mater. Interfaces

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Biomineralization is the process by which biological systems synthesize inorganic materials. Herein, we demonstrate an engineered cystathionine γ-lyase enzyme, smCSE that is active for the direct aqueous phase biomineralization of CdSe and CdSe-CdS core-shell nanocrystals. The nanocrystals are formed in an otherwise unreactive buff ered solution of Cd acetate and selenocystine through enzymatic turnover of the selenocystine to form a reactive precursor, likely H2Se. The particle size of the CdSe core nanocrystals can be tuned by varying the incubation time to generated particle sizes between 2.74 ± 0.63 nm and 4.78 ± 1.16 nm formed after 20 min and 24 h of incubation, respectively. Subsequent purification and introduction of L-cysteine as a sulfur source facilitates the biomineralization of a CdS shell onto the CdSe cores. The quantum yield of the resulting CdSe-CdS core-shell particles is up to 12% in the aqueous phase; comparable to that reported for more traditional chemical synthesis routes for core-shell particles of similar size with similar shell coverage. This single-enzyme route to functional nanocrystals synthesis reveals the powerful potential of biomineralization processes.

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Biomanufacturing of CdS quantum dots

Abstract: A strain of Stenotrophomonas maltophilia is engineered to achieve size controlled synthesis of water soluble CdS quantum dots.

Cited by 76 publications

References 51 publications

Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties

Single-enzyme biomineralization of cadmium sulfide nanocrystals with controlled optical properties

Biosynthesis of cadmium sulphide quantum dots by usingPleurotus ostreatus(Jacq.) P. Kumm

Single Enzyme Direct Biomineralization of CdSe and CdSe-CdS Core-Shell Quantum Dots

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