Tyrosinase-catalyzed modification of Bombyx mori silk fibroin: Grafting of chitosan under heterogeneous reaction conditions

Freddi, Giuliano; Anghileri, A.; Sampaio, Sandra; Büchert, Johanna; Monti, Patrizia; Taddei, Paola

doi:10.1016/j.jbiotec.2006.03.003

Cited by 133 publications

(97 citation statements)

References 39 publications

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“…[10][11][12][13][14][15][16] Second, tyrosinase activates accessible tyrosine residues of the C-terminal pentatyrosine pro-tag into reactive o-quinones, which then covalently link to the nucleophilic amine groups of chitosan to form the protein-chitosan conjugate. [16][17][18][19][20] Chitosan confers its pH-responsive properties to the protein upon covalent conjugation.…”

Section: Introductionmentioning

confidence: 99%

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Lewandowski

Bentley

et al. 2008

Biotechnology Progress

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in Wiley InterScience (www.interscience.wiley.com).We report an approach for spatially selective assembly of an enzyme onto selected patterns of microfabricated chips. Our approach is based on electrodeposition of the aminopolysaccharide chitosan onto selected electrode patterns and covalent conjugation of a target enzyme to chitosan upon biochemical activation of a genetically fused ''pro-tag.'' We report assembly of S-adenosylhomocysteine nucleosidase (Pfs) fused with a C-terminal pentatyrosine pro-tag. Pfs is a member of the bacterial autoinducer-2 biosynthesis pathway, catalyzing the irreversible cleavage of S-adenosylhomocysteine. The assembled Pfs retains its catalytic activity and structure, as demonstrated by retained antibody recognition. Assembly is controlled by the electrode area, resulting in reproducible rates of catalytic conversion for a given area, and thus allowing for area-based manipulation of catalysis and small molecule biosynthesis. Our approach enables optimization of small molecule biosynthesis in 1-step as well as multistep enzymatic reactions, including entire metabolic pathways, and we envision a wide variety of potential applications.

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Section: Introductionmentioning

confidence: 99%

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Lewandowski

Bentley

et al. 2008

Biotechnology Progress

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“…The mechanism of protein-chitosan conjugation has been investigated and proposed according to a reaction scheme recently developed for the silk-fibroin chitosan polymer system [35].…”

Section: Tyrosinase In Biomedical Applicationsmentioning

confidence: 99%

Biomimetic Materials for Medical Application Through Enzymatic Modification

Gentile

Chiono

Tonda‐Turo

et al. 2010

Biofunctionalization of Polymers and Their Applications

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Living organisms synthesize functional materials, based on proteins and polysaccharides, using enzyme-catalyzed reactions. According to the biomimetic approach, biomaterial matrices for tissue engineering are designed to be able to mimic the properties and the functions of the extracellular matrix (ECM). In this chapter, the most significant research efforts dedicated to the study and the preparation of biomimetic materials through enzymatic modifications were reviewed. The functionalizations of different polymeric matrices obtained through the catalytic activity of two enzymes (Transglutaminase, TGase and Tyrosinase, TYRase) were discussed. Specifically, the biomimetic applications of TGase and TYRase to confer appropriate biomimetic properties to the biomaterials, such as the possibility to obtain in situ gelling hydrogels and the incorporation of bioactive molecules (growth factors) and cell-binding peptides into the scaffolds, were reviewed.

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“…Since silk fibroin contains up to 10 % of tyrosine [14], tyrosinase might have the potential for silk functionalization by introducing amine functional compounds into fibroins. Meanwhile, the use of tyrosinase has been documented for covalently grafting of the polysaccharide of chitosan onto silk gels [15].…”

Section: Introductionmentioning

confidence: 99%

Enzymatic grafting of lactoferrin onto silk fibroins for antibacterial functionalization

et al. 2014

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Enzymatic oxidation of tyrosine side-chains in proteins could produce reactive o-quinones that might subsequently react with the primary amino groups of functional compounds, which provided a worthwhile reference for functionalization of fibrion materials. In the present work the potential for using tyrosinase to graft the bovine lactoferrin onto Bombyx mori silk fibroin was examined. Lactoferrin could adsorb onto silk fibers and covalently bind to the previous enzymatically oxidized fibroin surface. The enzyme-generated quinones in silk fibers also might cause self-crosslinking of fibroin peptides, which led to beneficial changes of silk properties. For the fabric treated with tyrosinase and lactoferrin slight improvements of dyeability and strength were obtained in comparison to the control. The combinedly treated fabric showed encouraging resistance to S. aureus and E. coli, the antibacterial activities reached to 87.0 % and 76.4 %, respectively. The durability of the antibacterial silk was noticeably higher than that of the sample treated with lactoferrin alone.

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Tyrosinase-catalyzed modification of Bombyx mori silk fibroin: Grafting of chitosan under heterogeneous reaction conditions

Cited by 133 publications

References 39 publications

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Towards area‐based in vitro metabolic engineering: Assembly of Pfs enzyme onto patterned microfabricated chips

Biomimetic Materials for Medical Application Through Enzymatic Modification

Enzymatic grafting of lactoferrin onto silk fibroins for antibacterial functionalization

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