Table of Contents
Journal of Nanoparticles
Volume 2013, Article ID 901401, 5 pages
Research Article

Coimmobilization of Naringinases on Silk Fibroin Nanoparticles and Its Application in Food Packaging

The State Engineering Laboratory of Modern Silk and Silk Biotechnology Key Laboratory, Medical College of Soochow University, No. 199, 702-2303 Room, Renai Road, Suzhou 215123, China

Received 8 November 2012; Accepted 30 December 2012

Academic Editor: Vijaya Rangari

Copyright © 2013 Min-Hui Wu et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


Bombyx mori silk fibroin is a macromolecular biopolymer with remarkable biocompatibility. It was degummed and subjected to a series of treatments, including dissolution and dialysis, to yield an aqueous solution of silk fibroin, which was introduced rapidly into excess acetone to produce crystalline silk fibroin nanoparticles (SFNs), which were conjugated covalently with naringinase using glutaraldehyde as the cross-linking reagent. The SFN naringinases are easily recovered by centrifugation and can be used repeatedly. Naringinase is a bienzyme consisting of α-L-rhamnosidase and flavonoid-β-glucosidase. The enzyme activity and its kinetics were similar to those of the native form, and the optimum reactive temperature for both is 55°C. In our study, centrifugation allowed the separation of enzyme and substrate; after eight cycles the SFN naringinases retained >70% residual activity. The highly efficient processing technology and the use of SFN as a novel vector for a bienzyme have great potential for research and the development of food processing such as the debittering of naringin-containing juices.