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

Authors

  • Sascha C. T. Nicklisch,

    Corresponding author
    1. Dept. of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA
    Current affiliation:
    1. University of California, San Diego, Scripps Institution of Oceanography, La Jolla, CA
    • Correspondence concerning this article should be addressed to S. C. T. Nicklisch at this current address: University of California, San Diego, Scripps Institution of Oceanography, 8750 Biological Grade Rd., 3155 Hubbs Hall, La Jolla, CA 92037; e-mail: snicklisch@ucsd.edu.

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  • Saurabh Das,

    1. Dept. of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA
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  • Nadine R. Martinez Rodriguez,

    1. Dept. of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA
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  • J. Herbert Waite,

    1. Dept. of Molecular, Cellular and Developmental Biology, University of California, Santa Barbara, CA
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  • Jacob N. Israelachvili

    1. Dept. of Chemical Engineering, University of California, Santa Barbara, CA
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  • This article was published online on 9 October 2013. An error was subsequently identified. This notice is included in the online and print versions to indicate that both have been corrected 29 October 2013.

Abstract

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. © 2013 American Institute of Chemical Engineers Biotechnol. Prog., 29:1587–1593, 2013

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