Antioxidant efficacy and adhesion rescue by a recombinant mussel foot protein-6

TitleAntioxidant efficacy and adhesion rescue by a recombinant mussel foot protein-6
Publication TypeJournal Article
Year of Publication2013
AuthorsNicklisch S.CT, Das S., Rodriguez N.RM, Waite J.H, Israelachvili J.N
JournalBiotechnology Progress
Date Published2013/11
Type of ArticleArticle
ISBN Number8756-7938
Accession NumberWOS:000328217100027
Keywordsadhesion rescue; antioxidant; cells; dopa; DOPA oxidation; protein; recombinant mussel; redox; thiol

Mytilus foot protein type 6 (mfp-6) is crucial for maintaining the reducing conditions needed for optimal wet adhesion in marine mussels. In this report, we describe the expression and production of a recombinant Mytilus californianus foot protein type 6 variant 1 (rmfp-6.1) fused with a hexahistidine affinity tag in Escherichia coli and its purification by affinity chromatography. Recombinant mfp-6 showed high purification yields of 5-6 mg L-1 cell culture and excellent solubility in low pH buffers that retard oxidation of its many thiol groups. Purified rmfp-6.1 protein showed high 2,2-diphenyl-1-picrylhydrazyl radical scavenging activity when compared with vitamin C. Using the highly sensitive surface forces apparatus (SFA) technique to measure interfacial surface forces in the nano-Newton range, we show that rmfp-6.1 is also able to rescue the oxidation-dependent adhesion loss of mussel foot protein 3 (mfp-3) at pH 3. The adhesion rescue is related to a reduction of dopaquinone back to 3,4-dihydroxyphenyl-l-alanine in mfp-3, which is the reverse reaction observed during the detrimental enzymatic browning process in fruits and vegetables. Broadly viewed, rmfp-6.1 has potential as a versatile antioxidant for applications ranging from personal products to antispoilants for perishable foods during processing and storage. (c) 2013 American Institute of Chemical Engineers Biotechnol. Prog., 29:1587-1593, 2013

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