Surface Modification of Cellulose Acetate with Cutinase and ...

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Influence of Mechanical Agitation on Cutinases and Protease Activity Toward Polyamide Substrates Control without discs Native without discs L182A without discs Subtilisin without discs Control with discs Native with discs L182A with discs Subtilisin with discs Figure 8. Scanning electronic microscopy (SEM) of samples treated with native, L182A mutant and proteases in the absence and in the presence of stainless steel discs. 4. Concluding remarks This study provided new insights about the influence of mechanical agitation on cutinase and protease activities towards polyamide substrates. The cutinase mutant (L182A) showed more ability to modify the surface of polyamide substrates when compared with the native one. However, the higher catalytic efficiency was obtained for protease due to its enzymatic specificity. The results obtained support the idea that when higher levels of mechanical agitation were introduced on the system the level of surface modification increased. The simultaneous action of the enzymes and the stainless steel discs lead to an increase of the enzymatic conversion, although a careful balance between the enzyme activity and the mechanical agitation is required to achieve higher level of hydrolysis without excessive fabric strength and weight loss. For a future industrial application of this process it is necessary to find this equilibrium. To produce the large amount of amino groups, short times of incubation must be used as well as vertical agitation. More studies have to be performed in order to predict and better control the polyamide finishing. 105
Subchapter 2.3 Acknowledgments The authors would like to thank Doctor Filipe Vaz, from University of Minho – Physics Department, for his help on the x-ray results discussion. This work was supported by the Biosyntex Project, nº G5RD-CT-2000-30110, from the European Community under the “Competitive and Sustainable Growth” Program, and by the PhD grant SFRH/BD/22490/2006, from Fundação para a Ciência e a Tecnologia (Portugal). 106
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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
Page 77 and 78: Subchapter 2.1 major material of co
Page 79 and 80: Subchapter 2.1 End uses include swe
Page 81 and 82: Subchapter 2.1 References Battistel
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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
Page 97 and 98: Mutation Subchapter 2.2 Table III.
Page 99 and 100: Subchapter 2.2 Table IV. Hydrophobi
Page 101 and 102: Subchapter 2.2 References Ansaldi M
Page 107 and 108: Subchapter 2.3 Abstract Two polyami
Page 109 and 110: Subchapter 2.3 aliphatic polyester.
Page 111 and 112: Subchapter 2.3 2.3. Determination o
Page 113 and 114: Subchapter 2.3 2.7. Enzymatic hydro
Page 115 and 116: Subchapter 2.3 The crystallinity va
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 125 and 126: Subchapter 2.3 Table II. Time of wa
Page 127: Subchapter 2.3 104 Abs 60 50 40 30
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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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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