Stabilization of enzymes in silk films

Shenzhou Lu, Xiaoqin Wang, Qiang Lu, Xiao Hu, Neha Uppal, Fiorenzo G. Omenetto, David L. Kaplan

Research output: Contribution to journalArticlepeer-review

138 Scopus citations

Abstract

Material systems are needed that promote stabilization of entrained molecules, such as enzymes or therapeutic proteins, without destroying their activity. We demonstrate that the unique structure of silk fibroin protein, when assembled into the solid state, establishes an environment that is conducive to the stabilization of entrained proteins. Enzymes (glucose oxidase, lipase, and horseradish peroxidase) entrapped in these films over 10 months retained significant activity, even when stored at 37 °C, and in the case of glucose oxidase did not lose any activity. Further, the mode of processing of the silk protein into the films could be correlated to the stability of the enzymes. The relationship between processing and stability offers a large suite of conditions within which to optimize such stabilization processes. Overall, the techniques reported here result in materials that stabilize enzymes to an extent, without the need for cryoprotectants, emulsifiers, covalent immobilization, or other treatments. Further, these systems are amenable to optical applications and characterization, environmental distribution without refrigeration, are ingestible, and offer potential use in vivo, because silk materials are biocompatible and FDA approved, degradable with proteases, and currently used in biomedical devices.

Original languageEnglish (US)
Pages (from-to)1032-1042
Number of pages11
JournalBiomacromolecules
Volume10
Issue number5
DOIs
StatePublished - May 11 2009

All Science Journal Classification (ASJC) codes

  • Bioengineering
  • Biomaterials
  • Polymers and Plastics
  • Materials Chemistry

Fingerprint Dive into the research topics of 'Stabilization of enzymes in silk films'. Together they form a unique fingerprint.

Cite this