Surface Modification of Cellulose Acetate with Cutinase and ...

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References Enzymatic Hydolysis of Wool with a Genetically Modified Subtilisin E Araújo R, Cavaco-Paulo A, Casal, M. 2008. Strategies towards the functionalization of Bacillus subtilis subtilisin E for wool finishing applications. Engineering in Life Sciences 8 (3):1-3. Brack N, Lamb R, Pham D, Turner P. 1999. Nonionic surfactants and the wool fibre surface. Colloids and Surfaces A- Physicochemical and Engineering Aspects 146:405–515. Cappello J, Crissman JW, Crissman M, Ferrari FA, Textor G, Wallis O, Whitledge JR, Zhou X, Burman D, Aukerman L, Stedronsky ER. 1998. In-situ self-assembling protein polymer gel systems for administration, delivery, and release of drugs. Journal of Controlled Release 53: 105–117. Girotti A, Reguera J, Rodríguez-Cabello JC, Arias FJ, Alonso M, Testera AM. 2004. Design and bioproduction of a recombinant multi(bio)functional elastin-like protein polymer containing cell adhesion sequences for tissue engineering purposes. Journal of Materials Science- Materials in Medicine 15(4):479-484. Rodríguez-Cabello JC, Reguera J, Girotti A, Alonso M, Testera AM. 2005. Developing Functionality in Elastin-Like Polymers by Increasing their Molecular Complexity: The Power of the Genetic Engineering Approach. Progress in Polymers Science 30 (11), 1119-1145. Inoue H, Nojima H, Okayama H. 1990. High efficiency transformation of Escherichia coli with plasmids. Gene 96:23-28. Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277:680-685. Lowry OH, Rosenberg WJ, Farr AL, Randell RJ. 1951. Quantitation of protein using Folin Ciocalteau reagent. Journal of Biological Chemistry193:265-75. Mahmoud Reza Banki, Liang Feng, David W Wood. 2005. Simple bioseparations using self-cleaving elastin-like polypeptide tags. Nature Methods 2 (9):659-661. Negri AP, Cornell HJ, Rivett DE. 1993. A model for the surface of keratin fibers. Textile Research Journal 63(2): 109-115. Sambroock J, Russel, DW. 2001. Molecular Cloning: A Laboratory Manual. In Cold Spring Harbor Laboratory, 3nd ed., Cold Spring Harbor, New York, NY. Sanger F, Nicklen S, Coulson AR. 1977. DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences of the United States of America 74:5463-5467. Shen J, Bishop DP, Heine E, Hollfelder B. 1999. Factors affecting the control of proteolytic enzyme reactions on wool. Journal of Textile Institute 90:404-411. Silva CJSM , Prabaharan M, Guebitz G, Cavaco-Paulo A. 2005. Treatment of wool fibres with subtilisin and subtilisin-PEG. Enzyme and Microbial Technology 36:917-922. Silva CJSM, Sousa F, Gübitz G, Cavaco-Paulo A. 2004. Chemical modifications on proteins using glutaraldehyde. Food Technology and Biotechnology 42:51-56. 215
Subchapter 3.3 Trabbic-Carlson K, Liu L, Kim B, Chilkoti A. 2004. Expression and purification of recombinant proteins from Escherichia coli: Comparison of an elastin-like polypeptide fusion with an oligohistidine fusion. Protein Science 13: 3274-3284. Urry, DW. 2006. What sustains life? Consilient mechanisms for protein-based machines and materials. Birkhauser Verlag. 216
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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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Subchapter 2.2 References Ansaldi M
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Subchapter 2.2 80
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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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Subchapter 2.4 118 TPA (mM) TPA (mM
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Subchapter 2.4 of native cutinase a
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Subchapter 2.4 122 K/S Increase (%)
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Subchapter 2.4 References Araújo R
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Subchapter 2.4 126
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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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Page 228 and 229: 1. Introduction Enzymatic Hydolysis
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Page 242 and 243: General Discussion and Future persp
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Page 246 and 247: References General Discussion and F
Page 248 and 249: Appendix
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