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Expression of Functional Recombinant Mussel Adhesive Protein Type 3A in Escherichia coli
Author(s) -
Hwang Dong Soo,
Gim Youngsoo,
Cha Hyung Joon
Publication year - 2008
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp050014e
Subject(s) - recombinant dna , bioadhesive , mussel , escherichia coli , adhesive , chemistry , affinity chromatography , adhesion , biochemistry , chromatography , biology , enzyme , organic chemistry , polymer , gene , ecology , layer (electronics)
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.