Surface Modification of Cellulose Acetate with Cutinase and ...

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Surface Modification of Cellulose Acetate with Cutinase and Cutinase Fused to Carbohydrate-binding Modules Surface Modification of Cellulose Acetate with Cutinase and Cutinase Fused to Carbohydrate-binding Modules TERESA MATAMÁ 1,2 , RITA ARAÚJO 2 , GEORG M GUEBITZ 3 , MARGARIDA CASAL 2 , ARTUR CAVACO-PAULO 1* 1 Center of Textile Engineering, University of Minho, Campus of Azurém, 4800-058 Guimarães, Portugal 2 CBMA Center of Environmental and Molecular Biology, Department of Biology, University of Minho, Campus of Gualtar, 4710-057 Braga, Portugal 3 Department of Environmental Biotechnology, Graz University of Technology, 8010 Graz, Austria Keywords: carbohydrate esterase, cutinase, surface modification, deacetylation, cellulose-binding domain *Correspondence to: Prof. Artur Cavaco-Paulo University of Minho – Textile Engineering Department 4800-058 Guimarães, Portugal Tel: +351 253 510271 Fax: +351 523 510293 E-mail: artur@det.uminho.pt 129
Subchapter 2.5 Abstract The surface of commercial cellulose diacetate and triacetate fabrics was modified with a cutinase (EC 3.1.1.74). The enzymatic hydrolysis of acetyl groups on the fibre surface was evaluated by the release of acetic acid and by the specific chemical staining of the fabrics with the cotton reactive dye Remazol Brilliant Blue R. The fabric treatment, during 8 hours at 30 ºC and pH 8, led to an acetyl esterase activity of 0.17 nkat and 0.12 nkat on cellulose diacetate and triacetate, respectively. The colour levels for samples treated with cutinase for 24 hours increased 25% for cellulose diacetate and 317% for cellulose triacetate, comparing to the control samples. Cross-sections of both fibres were analysed by fluorescence microscopy and confirmed the superficial action of cutinase. Crystallinity of both fibres was slightly decreased as a result of the enzymatic treatment. For further improvement of cutinase catalysis, fusion cutinases at the Cterminal ends were produced with either the carbohydrate-binding module of Cellobiohydrolase I, from the fungi Trichoderma reesei, or the carbohydrate-binding module of Endoglucanase C, from the bacteria Cellulomonas fimi. The knew recombinant cutinase fused to the fungal CBM was better than the bacterial one in improving the colour levels of treated fabrics, in particular for cellulose diacetate. In this work, evidences are provided showing that cutinase is a good candidate for superficial regeneration of cellulose hydrophilicity and reactivity on highly substituted cellulose acetates, although further studies will be necessary to better characterize the nature of the fibre transformations induced by the modular cutinases. Nomenclature: C.I. - Colour Index CBH I - Cellobiohydrolase I of Trichoderma reesei CDA - Cellulose diacetate CenA - Endoglucanase A of Cellulomonas fimi CenC - Endoglucanase C of Cellulomonas fimi CTA - Cellulose triacetate DS - degree of substitution K/S - Kubelka-Munk relationship: K - adsorption coefficient, S - scattering coefficient o.w.f. - of weight of fabric 130
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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 2.1 60
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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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Page 107 and 108: Subchapter 2.3 Abstract Two polyami
Page 109 and 110: Subchapter 2.3 aliphatic polyester.
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Page 113 and 114: Subchapter 2.3 2.7. Enzymatic hydro
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Page 117 and 118: Subchapter 2.3 Table I. Protein ads
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Page 129 and 130: Subchapter 2.3 Acknowledgments The
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Page 135 and 136: Subchapter 2.4 Abstract The effect
Page 137 and 138: Subchapter 2.4 A balance between en
Page 139 and 140: Subchapter 2.4 flask with stirring
Page 141 and 142: Subchapter 2.4 118 TPA (mM) TPA (mM
Page 143 and 144: Subchapter 2.4 of native cutinase a
Page 145 and 146: Subchapter 2.4 122 K/S Increase (%)
Page 147 and 148: Subchapter 2.4 References Araújo R
Page 154 and 155: Surface Modification of Cellulose A
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Page 184 and 185: SubChapter 3.1 Introduction
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Page 188 and 189: Enzymatic Modification of Wool Surf
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Strategies Towards the Functionaliz
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4. Discussion Strategies Towards th
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References Strategies Towards the F
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Subchapter 3.3 Enzymatic Hydolysis
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Enzymatic Hydolysis of Wool with a
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1. Introduction Enzymatic Hydolysis
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References Enzymatic Hydolysis of W
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Chapter 4 General Discussion and Fu
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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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