Surface Modification of Cellulose Acetate with Cutinase and ...

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Influence of Mechanical Agitation on Cutinases and Protease Activity Toward Polyamide Substrates Influence of Mechanical Agitation on Cutinases and Protease Activity Towards Polyamide Substrates CARLA SILVA 1 , RITA ARAÚJO 2 , MARGARIDA CASAL 2 , GEORG M. GÜBITZ 3 , 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 Graz University of Technology, Department of Environmental Biotechnology, 8010 Graz, Austria Kewords: polyamide, cutinase, protease, hydrolysis *Correspondence to: Prof. Artur Cavaco-Paulo University of Minho, Textile Engineering Department 4800-058 Guimarães, Portugal Tel: +351 253 510271 Fax: +351 253 510293 E-mail: artur@det.uminho.pt 83
Subchapter 2.3 Abstract Two polyamide 6,6 substrates with different construction, namely a model substrate and a fabric, were hydrolyzed using native cutinase and L182A cutinase mutant (from Fusarium solani pisi) and a protease (subtilisin from Bacillus sp.). The catalytic efficiency of these enzymes, measured in terms of hydrolysis products release, was measured for both substrates and the protease released 5 times more amines to the bath treatment. The L182A cutinase mutant showed higher activity when compared with the native enzyme. All enzymes have shown activity additive effects with higher levels of mechanical agitation for polyamide fabrics. The results achieved are of paramount importance on the design of a process of enzymatic functionalization of polyamide 84
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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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Page 56 and 57: References General Introduction: Ap
Page 58 and 59: General Introduction: Application o
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Page 77 and 78: Subchapter 2.1 major material of co
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Page 81 and 82: Subchapter 2.1 References Battistel
Page 87 and 88: Subchapter 2.2 Abstract Cutinase fr
Page 89 and 90: Subchapter 2.2 2. Materials and met
Page 91 and 92: Subchapter 2.2 Scheme 1. Thermodyna
Page 93 and 94: Subchapter 2.2 14000 rpm at 4 ºC.
Page 95 and 96: Subchapter 2.2 3. Results and discu
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Page 101 and 102: Subchapter 2.2 References Ansaldi M
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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 121 and 122: Subchapter 2.3 98 Protein in soluti
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Page 127 and 128: Subchapter 2.3 104 Abs 60 50 40 30
Page 129 and 130: Subchapter 2.3 Acknowledgments The
Page 131 and 132: Subchapter 2.3 Lau Y, Bruice C. 199
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 152 and 153: Surface Modification of Cellulose A
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Surface Modification of Cellulose A
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Chapter 3 Enzymatic Modification of
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SubChapter 3.1 Introduction
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1. Properties of Wool Enzymatic Mod
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Enzymatic Modification of Wool Surf
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3.3. Bleaching Enzymatic Modificati
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Subchapter 3.2 Strategies Towards t
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Strategies Towards the Functionaliz
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1. Introduction Strategies Towards
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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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