expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli
SCIE
SCOPUS
- Title
- expression of functional recombinant mussel adhesive protein type 3A in Escherichia coli
- Authors
- Hwang, DS; Gim Young Soo; CHA, HYUNG JOON
- Date Issued
- 2005-05
- Publisher
- Wiley
- Abstract
- Mussel adhesive proteins, including the 20-plus variants of foot protein type 3 (fp-3), have been suggested as potential environmentally friendly adhesives for use in aqueous conditions and in medicine. Here we report the novel production of a recombinant Mytilus galloprovincialis foot protein type 3 variant A (Mgfp-3A) fused with a hexahistidine affinity ligand in Escherichia coli and its ∼ 99% purification with affinity chromatography. Recombinant Mgfp-3A showed a superior purification yield and better apparent solubility in 5% acetic acid (prerequisites for large-scale production and practical use) compared to those of the previously reported recombinant M. galloprovincialis foot protein type 5 (Mgfp-5). The adsorption abilities and adhesion forces of purified recombinant Mgfp-3A were compared with those of Cell-Tak (a commercial mussel extract adhesive) and recombinant Mgfp-5 using quartz crystal microbalance analysis and modified atomic force microscopy, respectively. These assays showed that the adhesive ability of recombinant Mgfp-3A was comparable to that of Cell-Tak but lower than that of recombinant Mgfp-5. Collectively, these results indicate that recombinant Mgfp-3A may be useful as a commercial bioadhesive or an adhesive ingredient in medical or underwater environments.
- Keywords
- ATOMIC-FORCE MICROSCOPE; MYTILUS-EDULIS-L; PLAQUE PROTEIN; FAMILY
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/25693
- DOI
- 10.1021/BP050014E
- ISSN
- 8756-7938
- Article Type
- Article
- Citation
- BIOTECHNOLOGY PROGRESS, vol. 21, no. 3, page. 965 - 970, 2005-05
- Files in This Item:
- There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.