Bioinspired preparation of polydopamine microcapsule for multienzyme system construction

Zhang, Lei, Shi, Jiafu, Jiang, Zhongyi, Jiang, Yanjun, Qiao, Shizhang, Li, Jian, Wang, Rui, Meng, Ruijie, Zhu, Yuanyuan and Zheng, Yang (2011) Bioinspired preparation of polydopamine microcapsule for multienzyme system construction. Green Chemistry, 13 2: 300-306. doi:10.1039/c0gc00432d


Author Zhang, Lei
Shi, Jiafu
Jiang, Zhongyi
Jiang, Yanjun
Qiao, Shizhang
Li, Jian
Wang, Rui
Meng, Ruijie
Zhu, Yuanyuan
Zheng, Yang
Title Bioinspired preparation of polydopamine microcapsule for multienzyme system construction
Journal name Green Chemistry   Check publisher's open access policy
ISSN 1463-9262
1463-9270
Publication date 2011-02-01
Year available 2010
Sub-type Article (original research)
DOI 10.1039/c0gc00432d
Open Access Status Not Open Access
Volume 13
Issue 2
Start page 300
End page 306
Total pages 7
Place of publication Cambridge, United Kingdom
Publisher Royal Society of Chemistry
Language eng
Subject 2304 Environmental Chemistry
2310 Pollution
Abstract Inspired by the structural organization of mitochondria and the bioadhesive principle, a simple and versatile approach to construct a multienzyme system is developed. More specifically, the multienzyme system is composed of a polydopamine (PDA) microcapsule scaffold and three spatially separated enzymes. The PDA microcapsules are prepared through the rapid, spontaneous self-polymerization of dopamine on the surface of CaCO(3) microparticle template, followed by dissolution of the template using EDTA. The wall thickness of the microcapsules can be tuned by the dopamine concentration in an aqueous solution. The three enzymes are respectively immobilized through physical encapsulation in the lumen, in situ entrapment within the wall and chemical attachment on the out surface under extremely mild conditions. As an example, a multienzyme system, containing alpha-amylase, beta-amylase and glucosidase, was constructed to convert starch into isomaltooligosaccharide, and the multienzyme system displays higher catalytic activity and enhanced operational stability. The method developed in this study will establish a powerful platform for the facile construction of multienzyme cascade systems.
Formatted abstract
Inspired by the structural organization of mitochondria and the bioadhesive principle, a simple and versatile approach to construct a multienzyme system is developed. More specifically, the multienzyme system is composed of a polydopamine (PDA) microcapsule scaffold and three spatially separated enzymes. The PDA microcapsules are prepared through the rapid, spontaneous self-polymerization of dopamine on the surface of CaCO3 microparticle template, followed by dissolution of the template using EDTA. The wall thickness of the microcapsules can be tuned by the dopamine concentration in an aqueous solution. The three enzymes are respectively immobilized through physical encapsulation in the lumen, in situ entrapment within the wall and chemical attachment on the out surface under extremely mild conditions. As an example, a multienzyme system, containing α-amylase, β-amylase and glucosidase, was constructed to convert starch into isomaltooligosaccharide, and the multienzyme system displays higher catalytic activity and enhanced operational stability. The method developed in this study will establish a powerful platform for the facile construction of multienzyme cascade systems.
© 2011 The Royal Society of Chemistry.
Keyword Surface-chemistry
Polymer capsules
Polyelectrolyte
Enzymes
Q-Index Code C1
Q-Index Status Confirmed Code
Grant ID 2009CB724705
20976127
B06006
Institutional Status UQ
Additional Notes First published on the web 06 Dec 2010.

Document type: Journal Article
Sub-type: Article (original research)
Collections: Official 2011 Collection
Australian Institute for Bioengineering and Nanotechnology Publications
 
Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 93 times in Thomson Reuters Web of Science Article | Citations
Scopus Citation Count Cited 98 times in Scopus Article | Citations
Google Scholar Search Google Scholar
Created: Sun, 27 Mar 2011, 10:09:51 EST