Enzymatic modification of wool with tyrosinase and peroxidase

Lantto, Raija; Heine, Elisabeth; Freddi, Giuliano; Lappalainen, Arja; Miettinen-Oinonen, Arja; Niku-Paavola, M-L.; Büchert, Johanna

doi:10.1533/joti.2004.0080

Cited by 27 publications

(17 citation statements)

References 19 publications

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“…The interesting chemical, physical, mechanical and biological properties of wool protein fibres have a great potential for the development of biomaterials, e.g., for medical applications like bioactive dressings, scaffolds, wound healing, isolation materials, etc. [2][3][4].…”

Section: Introductionmentioning

confidence: 99%

“…In the presence of catechol, benzoquinone is formed [12]. Tyrosinase is capable of oxidising tyrosine residues in proteins to the corresponding quinones, which can further react with, e.g., free sulfhydryl (thiol) and/or amino groups, resulting in formation of tyrosine-cysteine and tyrosine-lysine cross-links [4,12,13].…”

Section: Introductionmentioning

confidence: 99%

“…It is believed that tyrosinase-catalyzed oxidation of tyrosyl or dihydroxyphenylalanine (DOPA) residues initiates cross-linking and gelation of adhesive proteins. Because quinones can undergo reactions with various moieties (e.g., tyrosyl residues and amino groups) and different linkages can be formed (e.g., Schiff base and Michaels-type adduct), the chemistry of quinone-tanning has not yet been fully established [4,12,13].…”

Section: Introductionmentioning

confidence: 99%

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

Jus

Kokol

Guebitz

2009

Journal of Biomaterials Science, Polymer Edition

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The potential of tyrosinases to activate tyrosine residues of wool protein fibres for cross-linking with different materials like collagen, elastin and gelatine was assessed. Natural fibres like wool offer an excellent environment for the growth of micro-organisms when the conditions like moisture, oxygen and temperature are appropriate. Coating with collagen, a very useful biomaterial with bactericidal and fungicidal properties, could be used to improve the properties of wool-based materials, especially when applied in hygienically sensitive applications like in hospitals. Tyrosinases were shown to catalyse the oxidation of tyrosine residues in wool and wool hydrolysates as model substrates, as determined by UV-Vis spectroscopy. Structural differences of the surface were evident from the increase of the intensity in the NH bending and stretching regions in the spectra of NIR FT Raman analysis of the enzyme treated and grafted wool fibres. The durability of the coating was also shown by using FITC-labelled collagen that was bound to the wool fibres, even after severe washing. Additionally, antimicrobial properties were successfully imparted due to the collagen grafted on the wool fibres. The functional and mechanical properties of the treated wool fibres showed no significant changes.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Jus

Kokol

Guebitz

2009

Journal of Biomaterials Science, Polymer Edition

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“…To date, different types of enzymesincluding proteases [7][8][9], lipases [10], laccases [11], peroxidase [12], tyrosinases [12,13], and transglutaminases [14][15][16][17]-have been used for improving the qualities of wool fabrics or providing new functions to wool. However, as far as our knowledge goes, no report has so far involved the enzymatically antibacterial functionalization of wool textiles.…”

Section: Introductionmentioning

confidence: 99%

Antibacterial Functionalization of Wool via mTGase-Catalyzed Grafting of ε-Poly-l-lysine

Wang

Jin

Fan

et al. 2009

Appl Biochem Biotechnol

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epsilon-Poly-L-lysine (epsilon-PL), a natural biomacromolecule having a broad spectrum of antibacterial activity, was grafted on the wool fiber via the acyl transfer reaction catalyzed by microbial transglutaminase (mTGase) to develop a new strategy for antibacterial functionalization of proteinous materials. The effects of the concentrations of epsilon-PLs and mTGases on the graft yields were investigated. A coating of epsilon-PL that almost completely covered the scale profile on the wool surface was visualized by scanning electron microscopy (SEM) and further demonstrated in terms of Allwörden's reaction characteristic of wool. Identifiable differences in lysine content and color depth among the stained wool samples reveal the changes in the surface composition and polarity caused by the incorporation of epsilon-PL onto the wool substrate, respectively. The ratio of bacteriostasis to Escherichia coli of the wool fabric grafting epsilon-PL reached 96.6 %, indicating an excellent antibacterial effect. The application of epsilon-PL and corresponding mTGase-catalyzed grafting reaction would provide a worthwhile reference for antibacterial functionalization of proteinous materials in various forms.

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“…For example, tyrosinase was used to catalyze crosslinking of chicken myofibril proteins forming a thermally stable gel (Lantto et al 2006). Lantto et al (2005) showed that, the mushroom enzyme, tyrosinase increased gelation of fibrous wool proteins giving products with improved physical properties. Particularly, they enhanced gel strengths (Bloom), increased melting points, viscosities, and temperature of gelation.…”

Section: Introductionmentioning

confidence: 99%

Gelling Properties of Tyrosinase-Treated Dairy Proteins

Onwulata

Tomasula

2008

Food Bioprocess Technol

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Protein-based viscous gels can augment or replace carbohydrate-based ones for specific nutritional formulations such as in reduced calorie or low-fat food applications. In this study, slurries of whey protein isolates and calcium caseinate mixed with alginic acid (20% T.S.) were subjected to high-shear homogenization (microparticulation) at 27,000 rpm for 2, 3, 4, and 6 min. The resulting slurries were incubated with mushroom tyrosinase (E.C. 1.14.18.1) at levels of 3, 6, and 9 mg/100 g for 15, 30, and 60 min to facilitate gel formation of the alginic acid with the homogenized dairy proteins. The results indicate that the time of high-shear homogenization had significant (P< 0.05) effect on the viscosities of the gels. Highest gel viscosity was obtained with 6 mg tyrosinase at 60 min, but increases in gel viscosity depended on time of shear, with 2 and 4 min shear resulting in higher viscosity (484 and 6,143 cP) and stronger complex viscosity (49 and 38 Pa.s at 1 rad/s), respectively, compared to the control (69 cP) and (12 Pa.s at 1 rad/s). Gels were stable in refrigerated storage up to 240 h, strengthened with time of refrigeration storage, and became significantly more viscoelastic. Optimal viscous properties were obtained at 4 min microparticulation, 60 min incubation, and 6 mg tyrosinase treatment.

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Enzymatic modification of wool with tyrosinase and peroxidase

Cited by 27 publications

References 19 publications

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

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

Antibacterial Functionalization of Wool via mTGase-Catalyzed Grafting of ε-Poly-l-lysine

Gelling Properties of Tyrosinase-Treated Dairy Proteins

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