Abstract
We investigated how a genetically engineered resilin fusion protein modifies cellulose surfaces. We characterized the pH-responsive behavior of a resilin-like polypeptide (RLP) having terminal cellulose binding modules (CBM) and showed its binding to cellulose nanofibrils (CNF). Characterization of the resilin fusion protein at different pHs revealed substantial conformational changes of the protein, which were observed as swelling and contraction of the protein layer bound to the nanocellulose surface. In addition, we showed that employment of the modified resilin in cellulose hydrogel and nanopaper increased their modulus of stiffness through a cross-linking effect.
MeSH terms
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Amino Acid Sequence
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Biocompatible Materials / chemistry*
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Cellulose / chemistry*
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Cloning, Molecular
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Elastic Modulus
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Elasticity
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Genetic Vectors / chemistry
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Genetic Vectors / metabolism
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Hydrogen-Ion Concentration
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Insect Proteins / biosynthesis
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Insect Proteins / chemistry*
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Insect Proteins / genetics
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Nanostructures / chemistry*
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Protein Binding
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Protein Engineering
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Recombinant Fusion Proteins / biosynthesis
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Recombinant Fusion Proteins / chemistry*
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Recombinant Fusion Proteins / genetics
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Trichoderma / genetics
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Trichoderma / metabolism
Substances
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Biocompatible Materials
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Insect Proteins
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Recombinant Fusion Proteins
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resilin
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Cellulose