Mussel adhesive proteins (MAPs) have been regarded as outstanding marine-derived biomaterials due to their biocompatibility, biodegradability, and adhesion ability to various surfaces. In order for MAP to crosslink and adsorb quickly in the tough sea environment, tyrosine residues of MAP are modified into 3,4-dihydroxyphenyl-L-alanines (L-DOPAs) by natural mechanism. In our previous research, fp-151, a recombinant MAP, was successfully over-expressed as a form of inclusion body in Escherichia coli. However, in vitro tyrosine modification was demanded after production for higher adhesion characteristic of fp-151. Instead of performing this additional treatment, in the present work, E. coli co-expression system of tyrosinase and fp-151 was constructed to modify tyrosine residues in vivo. In this method, fp-151 was over-expressed and mainly obtained not from inclusion body, but from soluble fraction. Furthermore, MALDI-MS/MS analysis of solubleexpressed fp-151 implies some of tyrosine residues were definitely modified. This study suggested one possible strategy for in vivo incorporation of modified tyrosine residues in MAPs. The approach is applicable for economic and efficient modification of tyrosine residues. Yoon Jeong YANG, Dooyup JUNG, Yoo Seong CHOI and Hyung Joon CHA* Department of Chemical Engineering, Pohang University of Science and Technology, Pohang, 790-784, Korea. PMB03 Comparison of Lipid Contents of Chlorella sp. MB01 and Chlorella sp. MB02 Cultivated in Various Media
한국생물공학회 [The Korean Society for Biotechnology and Bioengineering]
설립연도
1984
분야
공학>생물공학
소개
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