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PRODUCTION OF FUSION MUSSEL ADHESIVE FP-353 IN ESCHERICHIA COLI

Title
PRODUCTION OF FUSION MUSSEL ADHESIVE FP-353 IN ESCHERICHIA COLI
Authors
Youngsoo GimHwang, DSSunghae LimYounghoon SongCHA, HYUNG JOON
POSTECH Authors
Hwang, DSCHA, HYUNG JOON
Date Issued
Nov-2008
Publisher
AMER CHEMICAL SOC
Abstract
Mussel adhesive proteins (MAPs) have a potential as environmentally friendly adhesives for use under aqueous conditions. MAPs maybe of particular value in medical applications. We previously reported the functional expression of recombinant foot protein type 5 (fp-5) and foot protein type 3A (fp-3A), both of which have significant adhesion abilities, in Escherichia coli. However, these proteins were produced at low levels because of post-induction cell growth inhibition, and the proteins showed poor post-purification solubility. Here, we design and produce a new, type of recombinant MAP, fp-353, that is a fusion protein with fp-3A at each terminus of fp-5. Because fp-353 formed inclusion bodies, host cell growth inhibition did not occur. In addition, the solubility of MAP fp-353 after purification was significantly enhanced, permitting the preparation of a viscous concentrated glue solution for large-scale adhesion strength measurements. Together with large-scale cowhide adhesion measurements and cell-adhesion analyses, we successfully demonstrated that fusion mussel protein fp-353 has potential as a practical alternative bioadhesive.
Mussel adhesive proteins (MAPs) have a potential as environmentally friendly adhesives for use under aqueous conditions. MAPs maybe of particular value in medical applications. We previously reported the functional expression of recombinant foot protein type 5 (fp-5) and foot protein type 3A (fp-3A), both of which have significant adhesion abilities, in Escherichia coli. However, these proteins were produced at low levels because of post-induction cell growth inhibition, and the proteins showed poor post-purification solubility. Here, we design and produce a new, type of recombinant MAP, fp-353, that is a fusion protein with fp-3A at each terminus of fp-5. Because fp-353 formed inclusion bodies, host cell growth inhibition did not occur. In addition, the solubility of MAP fp-353 after purification was significantly enhanced, permitting the preparation of a viscous concentrated glue solution for large-scale adhesion strength measurements. Together with large-scale cowhide adhesion measurements and cell-adhesion analyses, we successfully demonstrated that fusion mussel protein fp-353 has potential as a practical alternative bioadhesive.
URI
http://oasis.postech.ac.kr/handle/2014.oak/25701
DOI
10.1021/BP.65
ISSN
8756-7938
Article Type
Article
Citation
BIOTECHNOLOGY PROGRESS, vol. 24, no. 6, page. 1272 - 1277, 2008-11
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 CHA, HYUNG JOON
Dept. of Chemical Enginrg
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