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Expression of Functional Recombinant Mussel Adhesive Protein Mgfp-5 in Escherichia coli

Title
Expression of Functional Recombinant Mussel Adhesive Protein Mgfp-5 in Escherichia coli
Authors
Hwang, DSYoo Hyo JinJong Hyub JunMOON, WON KYUCHA, HYUNG JOON
POSTECH Authors
Hwang, DSMOON, WON KYUCHA, HYUNG JOON
Date Issued
Jun-2004
Publisher
American Society for Microbiology
Abstract
Mussel adhesive proteins have been suggested as a basis for environmentally friendly adhesives for use in aqueous conditions and in medicine. However, attempts to produce functional and economical recombinant mussel adhesive proteins (mainly foot protein type 1) in several systems have failed. Here, the cDNA coding for Mytilus galloprovincialis foot protein type 5 (Mgfp-5) was isolated for the first time. Using this cDNA, we produced a recombinant Mgfp-5 fused with a hexahistidine affinity ligand, which was expressed in a soluble form in Escherichia coli and was highly purified using affinity chromatography. The adhesive properties of purified recombinant Mgfp-5 were compared with the commercial extracted mussel adhesive Cell-Tak by investigating adhesion force using atomic force microscopy, material surface coating, and quartz crystal microbalance. Even though further macroscale assays are needed, these microscale assays showed that recombinant Mgfp-5 has significant adhesive ability and may be useful as a bioadhesive in medical or underwater environments.
Mussel adhesive proteins have been suggested as a basis for environmentally friendly adhesives for use in aqueous conditions and in medicine. However, attempts to produce functional and economical recombinant mussel adhesive proteins (mainly foot protein type 1) in several systems have failed. Here, the cDNA coding for Mytilus galloprovincialis foot protein type 5 (Mgfp-5) was isolated for the first time. Using this cDNA, we produced a recombinant Mgfp-5 fused with a hexahistidine affinity ligand, which was expressed in a soluble form in Escherichia coli and was highly purified using affinity chromatography. The adhesive properties of purified recombinant Mgfp-5 were compared with the commercial extracted mussel adhesive Cell-Tak by investigating adhesion force using atomic force microscopy, material surface coating, and quartz crystal microbalance. Even though further macroscale assays are needed, these microscale assays showed that recombinant Mgfp-5 has significant adhesive ability and may be useful as a bioadhesive in medical or underwater environments.
URI
http://oasis.postech.ac.kr/handle/2014.oak/29744
DOI
10.1128/AEM.70.6.3352-3359.2004
ISSN
0099-2240
Article Type
Article
Citation
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, vol. 70, no. 6, page. 3352 - 3359, 2004-06
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 CHA, HYUNG JOON
Dept. of Chemical Enginrg
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