Tyrosinase-Catalysed Coating of Wool Fibres With Different Protein-Based Biomaterials

Jus, Suzana; Kokol, Vanja; Guebitz, Georg M.

doi:10.1163/156856209x404523

Cited by 30 publications

(15 citation statements)

References 29 publications

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“…In a similar approach, wool fibers have been functionalized with ε-linked polylysine, an FDA-approved biomolecule with antibacterial properties (Wang et al 2010). Recent studies demonstrated that tyrosinase can be employed to oxidize tyrosyl side chains of keratin, allowing crosslinking of proteins such as collagen and elastin to wool fibers (Jus et al 2009; Lantto et al 2012). In the leather industry, transglutaminase-crosslinked preparations of gelatin and casein have been examined as low-cost filling materials to stuff voids in animal hides.…”

Section: Formation Of Protein Networkmentioning

confidence: 99%

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

250

190

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The process of protein crosslinking comprises the chemical, enzymatic, or chemoenzymatic formation of new covalent bonds between polypeptides. This allows (1) the site-directed coupling of proteins with distinct properties and (2) the de novo assembly of polymeric protein networks. Transferases, hydrolases, and oxidoreductases can be employed as catalysts for the synthesis of crosslinked proteins, thereby complementing chemical crosslinking strategies. Here, we review enzymatic approaches that are used for protein crosslinking at the industrial level or have shown promising potential in investigations on the lab-scale. We illustrate the underlying mechanisms of crosslink formation and point out the roles of the enzymes in their natural environments. Additionally, we discuss advantages and drawbacks of the enzyme-based crosslinking strategies and their potential for different applications.

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Section: Formation Of Protein Networkmentioning

confidence: 99%

Enzyme-catalyzed protein crosslinking

Heck

Faccio

Richter

et al. 2012

Appl Microbiol Biotechnol

250

190

View full text Add to dashboard Cite

show abstract

“…Recently, enzymes are being more fully enlisted for the fabrication and modification of materials [161][162][163][164][165][166][167][168][169][170][171][172][173][174][175][176][177]. Oxidative enzymes especially, tyrosinases, laccases, and peroxidases have been used to generate derivatives of chitosan [178][179][180] and have been extended to generating protein-chitosan conjugates [181].…”

Section: Biofunctionalizing Electrodeposited Chitosan Filmsmentioning

confidence: 99%

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

et al. 2014

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Individually, advances in microelectronics and biology transformed the way we live our lives. However, there remain few examples in which biology and electronics have been interfaced to create synergistic capabilities. We believe there are two major challenges to the integration of biological components into microelectronic systems: (i) assembly of the biological components at an electrode address, and (ii) communication between the assembled biological components and the underlying electrode. Chitosan OPEN ACCESSPolymers 2015, 7 2 possesses a unique combination of properties to meet these challenges and serve as an effective bio-device interface material. For assembly, chitosan's pH-responsive film-forming properties allow it to "recognize" electrode-imposed signals and respond by self-assembling as a stable hydrogel film through a cathodic electrodeposition mechanism. A separate anodic electrodeposition mechanism was recently reported and this also allows chitosan hydrogel films to be assembled at an electrode address. Protein-based biofunctionality can be conferred to electrodeposited films through a variety of physical, chemical and biological methods. For communication, we are investigating redox-active catechol-modified chitosan films as an interface to bridge redox-based communication between biology and an electrode. Despite significant progress over the last decade, many questions still remain which warrants even deeper study of chitosan's structure, properties, and functions.

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“…Due to the ability of tyrosinases to react with phenols, these enzymes have been proposed for the uses in a variety of biotechnological, biosensor and biocatalysis applications [1,8,9]. For example, tyrosinases can be applied in detoxification of phenol-containing wastewater and contaminant soils [10], synthesis of L-3,4-dihydroxyphenylalanine (L-DOPA), one of the preferred drugs for the treatment of Parkinson‘s disease [11], or as additives in food processes due to their cross-linking abilities [12,13].…”

Section: Introductionmentioning

confidence: 99%

High level production of tyrosinase in recombinant Escherichia coli

et al. 2013

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BackgroundTyrosinase is a bifunctional enzyme that catalyzes both the hydroxylation of monophenols to o-diphenols (monophenolase activity) and the subsequent oxidation of the diphenols to o-quinones (diphenolase activity). Due to the potential applications of tyrosinase in biotechnology, in particular in biocatalysis and for biosensors, it is desirable to develop a suitable low-cost process for efficient production of this enzyme. So far, the best production yield reported for tyrosinase was about 1 g L-1, which was achieved by cultivating the filamentous fungus Trichoderma reesei for 6 days.ResultsIn this work, tyrosinase from Verrucomicrobium spinosum was expressed in Escherichia coli and its production was studied in both batch and fed-batch cultivations. Effects of various key cultivation parameters on tyrosinase production were first examined in batch cultures to identify optimal conditions. It was found that a culture temperature of 32 °C and induction at the late growth stage were favorable, leading to a highest tyrosinase activity of 0.76 U mL-1. The fed-batch process was performed by using an exponential feeding strategy to achieve high cell density. With the fed-batch process, a final biomass concentration of 37 g L-1 (based on optical density) and a tyrosinase activity of 13 U mL-1 were obtained in 28 hours, leading to a yield of active tyrosinase of about 3 g L-1. The highest overall volumetric productivity of 103 mg of active tyrosinase per liter and hour (corresponding to 464 mU L-1 h-1) was determined, which is approximately 15 times higher than that obtained in batch cultures.ConclusionsWe have successfully expressed and produced gram quantities per liter of active tyrosinase in recombinant E. coli by optimizing the expression conditions and fed-batch cultivation strategy. Exponential feed of substrate helped to prolong the exponential phase of growth, to reduce the fermentation time and thus the cost. A specific tyrosinase production rate of 103 mg L−1 h−1 and a maximum volumetric activity of 464 mU L−1 h-1 were achieved in this study. These levels have not been reported previously.

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Tyrosinase-Catalysed Coating of Wool Fibres With Different Protein-Based Biomaterials

Cited by 30 publications

References 29 publications

Enzyme-catalyzed protein crosslinking

Enzyme-catalyzed protein crosslinking

Chitosan to Connect Biology to Electronics: Fabricating the Bio-Device Interface and Communicating Across This Interface

High level production of tyrosinase in recombinant Escherichia coli

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