alexa Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the
ISSN: 2157-7544

Journal of Thermodynamics & Catalysis
Open Access

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Research Article

Stellate MSN-based Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products

Hao-Hsin Chi1, Daniela R Radu1,2, Geraldine Dezayas1,3, Miranda Penney1,3 and Cheng-Yu Lai1*

1Department of Chemistry, Delaware State University, 1200 N. DuPont Highway, Dover, DE, 19901, USA

2Department of Materials Science and Engineering, University of Delaware, Newark, DE, 19716, USA

3Department of Biological Sciences, Delaware State University, 1200 N. DuPont Highway, Dover, DE, 19901, USA

*Corresponding Author:
Cheng-Yu Lai
Department of Chemistry, Delaware State University
1200 N. DuPont Highway, Dover, DE, 19901
Tel: 13028576537
E-mail: [email protected]

Received date: April 25, 2017; Accepted date: April 30, 2017; Published date: May 03, 2017

Citation: Chi HH, Radu DR, Dezayas G, Penney M, Lai CY (2017) Stellate MSNbased Dual-enzyme Nano-Biocatalyst for the Cascade Conversion of Non-Food Feedstocks to Food Products. J Thermodyn Catal 8: 185. doi: 10.4179/2160- 7544.1000185

Copyright: © 2017 Chi HH, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.



The successful demonstration of a tandem enzymatic catalyst which utilizes stellate macroporous silica nanospheres (Stellate MSN) platform as dual-enzyme host is reported herein. Upon simultaneous loading of beta-glucosidase and glucose isomerase inside their porous structure, Stellate MSNs-featuring a hierarchical pore arrangement and large surface area, show capability to perform a cascade reaction that converts cellobiose, a cellulosic hydrolysis product, into glucose and further to fructose. The silica platform provides a modality for substrate channelling which involves the transfer of the cascade intermediate, glucose, to the next enzyme without first diffusing to the bulk. A key aspect to this proof-of-concept is the two-enzyme system working in an optimized pH domain to fit the modus operandi for both enzymes. The concept could be extrapolated to other enzyme tandems, with potential to impact dramatically enzymatic processes which require multi-catalyst, one-pot transformations.


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