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• W2070614259 endingPage "150" @default.
• W2070614259 startingPage "143" @default.
• W2070614259 abstract "Enzymatic cross-linking of proteins can be catalyzed either by transferase-type enzymes, e.g., transglutaminases, or by oxidoreductases, e.g., tyrosinases or laccases. Three-dimensional structure of protein substrate plays a key role in these reactions, that is, the reactivity and end product are strongly modulated by the accessibility of target amino acid residues to the cross-linking enzyme. Typically structural integrity of protein can be distorted by heat, pH, or mechanical action, as well as by varying ionic concentration of the solution. In this study we used partially unfolded protein (wild-type DrkN SH3) and its structurally stabilized mutant (T22G) to investigate the impact of folded/unfolded conformations on cross-linking by Trichoderma reesei tyrosinase. Our results clearly showed formation of intermolecular cross-links solely between unfolded conformations, making them superior substrates to folded proteins when using tyrosinase as a cross-linking enzyme. Multidimensional heteronuclear magnetic resonance experiments in solution state were employed to investigate cross-linked end-products. The results presented in this study form basis for application development in food, medical, cosmetic, textile, packing and other sectors. In addition, the outcome of this study has a high value for the basic understanding of reaction mechanism of tyrosinases on proteins." @default.
• W2070614259 created "2016-06-24" @default.
• W2070614259 creator A5011357550 @default.
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• W2070614259 date "2011-01-01" @default.
• W2070614259 modified "2023-10-16" @default.
• W2070614259 title "Effect of protein structural integrity on cross-linking by tyrosinase evidenced by multidimensional heteronuclear magnetic resonance spectroscopy" @default.
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• W2070614259 doi "https://doi.org/10.1016/j.jbiotec.2010.11.006" @default.
• W2070614259 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21087642" @default.
• W2070614259 hasPublicationYear "2011" @default.
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