Surface Modification of Cellulose Acetate with Cutinase and ...

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Enzymatic Modification of Wool Surface - Introduction surface specific because the reaction with the cuticle takes place in less than 10 seconds. Chlorination results in the oxidation of cystine residues to cysteic acid residues in the surface of the fiber and allows the Hercosett 125 polymer, applied afterwards, to spread and adhere evenly along the fibre surface (Heine, 2002). This polymer, which is normally used to improve the wet strength of paper products, swells to 10x its normal thickness in water thus preventing the scale edges of adjacent fibres from interacting and causing felting during washing. The chlorine-Hercosett process has been employed in the industry for the last 30 years, and about of 75% of the world's treated wool is processed by this route in one of its forms (Holme, 2003). As previously mentioned (Chapter 1) this process has excellent advantages (antifelt effect, low damage and low weight loss) but it also shows a number of drawbacks like limited durability, poor handle, yellowing of wool, difficulties in dyeing and the most important today, release of absorbable organic halogens (AOX) to the effluents (Heine, 2002; Schlink and Greeff, 2001). There is therefore an increasing demand for environmentally friendly alternatives. 4. Enzymatic Finishing Processes for Wool Enzymes can be used in order to develop environmentally friendly alternative processes. Since wool mainly consists of proteins and lipids especially proteases and lipases have been investigated for wool fibre modification. However, the complex structure of natural fibres, especially of wool, brings complexicity to enzymatic fibre modification. Proteases and lipases can catalyse the degradation of different fibre components of wool preventing an accurate control of the reaction. If not controlled, this diffusion leads to a strong damage of the wool fibre, being crucial to restrict the enzymatic action to the wool fibre surface. The following subchapters describe the approaches developed in the scope of this thesis aiming to restrict subtilisin E hydrolysis to the surface of wool. 169
Subchapter 3.1 References Brack N, Lamb R, Pham D, Turner P. 1999. Nonionic surfactants and the wool fibre surface. Colloids and Surfaces. A: Physicochemical and Engineering Aspects 146: 405-415. Feughelman M. 1997. Introduction to the physical properties of wool, hair & other α– keratin fibres. In: Mechanical properties and structure of alpha-keratin fibres: wool, human hair and related fibres, UNSW Press, 1-14. Gacen J, Cayuela D. 2000. Comparison of wool bleaching with hydrogen peroxide in alkaline and acidic media. Journal of Society of Dyers and Colourits 116: 13-15. Han S, Yang Y. 2005. Antimicrobial activity of wool fabric treated with curcumin. Dyes and Pigments 64: 157-161. Heine E, Höcker H. 1995. Enzyme treatments for wool and cotton. Review of Progress of Coloration 25: 57-63. Heine E. 2002. Shrinkproofing and handle modification of wool. Newsletter WG4/1, COST 847 ‘Textile Biotechnology and Quality’ 1: 6-10. Holme I. 2003. Challenge and change in wool dyeing and finishing. Review of Progress of Coloration 33: 85-92. Lewis, DM. 1992. Ancilliary processes in wool dyeing. In: Wool Dyeing, Ed. Lewis, DM. Bradford: Society of Dyers and Colourists, 111-136. Makinson KR. 1979. Shrinkproofing of wool. Marcel Dekker Inc., New York, Basel, 373p. Naik S, Speakman PT. 1993. Associations between intermediate filament and intermediate filament associated protein and membrane protein, in wool. Biochemical Society Transactions 21: 279-283. Naik S. 1994. Study of naturally crosslinked protein from wool, including membrane protein. Ph.D. Thesis, University of Leeds. Negri AP, Cornell HJ, Rivett DE. 1993. A model for the surface of keratin fibers. Textile Research Journal 63(2): 109-115. Pailthorpe MT. 1992. The theoretical basis for wool dyeing. In: Wool Dyeing, Lewis, DM. Bradford: Society of Dyers and Colourists, 52-87. Pearson J, Lu F, Gandhi K. 2004. Disposal of wool scouring sludge by composting. AUTEX Research Journal 4(3): 147-156. Plowman JE. 2003. Proteomic database of wool components. Journal of Chromatography B 787: 63-76. Purwar R, Joshi M. 2004. Recent developments in antimicrobial finishing of textiles – a review. AATCC review, 22-26. Rippon JA. 1992. The structure of wool. In: Wool Dyeing, Ed. Lewis, DM. Bradford: Society of Dyers and Colourists, 1-51. Sawada K, Ueda M. 2001. Enzyme processing of textiles in reverse micellar solution. Journal of Biotechnology 89: 263-269. 170
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Universidade do Minho Escola de Ci
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É AUTORIZADA A REPRODUÇÃO PARCIA
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Acknowledgments/ Agradecimentos
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Às 2 mosqueteiras ausentes, Joana
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Abstract The challenges facing the
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Resumo
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Resumo Os desafios que a indústria
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molecular ficou retida à superfíc
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Table of contents Acknowledgments /
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CATs- Catalases CBD- Carbohydrate b
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Chapter 1 General Introduction: App
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General Introduction: Application o
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1. Biotechnology in textile industr
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3. Role of enzymes in textile indus
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7. Serine proteases: subtilisins Ge
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12.1 Decolourization of dyes and te
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References General Introduction: Ap
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Chapter 2 Surface Modification of S
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Subchapter 2.1 52
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Subchapter 2.1 major material of co
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Subchapter 2.1 End uses include swe
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Subchapter 2.1 References Battistel
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Subchapter 2.2 62
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Subchapter 2.2 Abstract Cutinase fr
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Subchapter 2.2 2. Materials and met
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Subchapter 2.2 Scheme 1. Thermodyna
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Subchapter 2.2 14000 rpm at 4 ºC.
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Subchapter 2.2 3. Results and discu
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Mutation Subchapter 2.2 Table III.
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Subchapter 2.2 Table IV. Hydrophobi
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Subchapter 2.2 References Ansaldi M
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Subchapter 2.3 82
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Subchapter 2.3 Abstract Two polyami
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Subchapter 2.3 aliphatic polyester.
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Subchapter 2.3 2.3. Determination o
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Subchapter 2.3 2.7. Enzymatic hydro
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Subchapter 2.3 The crystallinity va
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Subchapter 2.3 Table I. Protein ads
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Subchapter 2.3 In the same set of e
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Subchapter 2.3 98 Protein in soluti
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Subchapter 2.3 100 Protein in solut
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Subchapter 2.3 Table II. Time of wa
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Subchapter 2.3 104 Abs 60 50 40 30
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Subchapter 2.3 Acknowledgments The
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Subchapter 2.3 Lau Y, Bruice C. 199
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Subchapter 2.4 110
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Subchapter 2.4 Abstract The effect
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Subchapter 2.4 A balance between en
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Subchapter 2.4 flask with stirring
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General Discussion and Future persp
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General Discussion and Future Persp
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References General Discussion and F
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Appendix
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SOB TE buffer Autoclave Tryptone 2%
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Dissolve the nucleic acids in 30 μ
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