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Covalently immobilized enzyme gradients within three‐dimensional porous scaffolds
Author(s) -
Vepari Charu P.,
Kaplan David L.
Publication year - 2006
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20833
Subject(s) - fibroin , carbodiimide , covalent bond , horseradish peroxidase , immobilized enzyme , chemistry , porosity , self healing hydrogels , biosensor , chemical engineering , tissue engineering , polymer , silk , polymer chemistry , materials science , enzyme , biochemistry , organic chemistry , biomedical engineering , composite material , engineering , medicine
Horseradish peroxide (HRP) was covalently coupled to three‐dimensional (3D) silk fibroin scaffolds using water‐soluble carbodiimide. Stable, bilaterally symmetrical immobilized HRP gradient patterns were generated within 3D silk fibroin scaffolds using the principles of diffusion. Gradients of immobilized HRP activity were controlled using variables of volume and concentration of HRP solution activated by the carbodiimide. The method developed can be extended to immobilize a variety of proteins and small molecules on several types of porous, interconnected materials. This technique of patterning enzymes and proteins in a gradient manner offers new options in the field of chemotaxis, tissue engineering, and biosensors. © 2006 Wiley Periodicals, Inc.