Surface Modification of Cellulose Acetate with Cutinase and ...

More documents

Recommendations

Info

Surface Modification of Cellulose Acetate with Cutinase and Cutinase Fused to Carbohydrate-binding Modules 7). The fusion of cutinase to the CBMs had a more pronounced effect for the less substituted acetate, independently of the CBM type. The steric constrains should be stronger in the triacetate fibre and consequently the interactions necessary for the ligand recognition by the CBM should be more impaired on this fibre surface regarding the diacetate fibre. Due to the fact that different initial amounts of protein were used, is not possible to compare directly the protein adsorption behaviour of the several constructs. But it is possible to see for this particular treatment that there was no obvious relation between the colour differences and the amount of protein adsorbed. Taking in account the different esterase activities used, the cutinase-wtCBMCBHI and cutinase-sCBMCBHI seem the most efficient catalysts under the treatment conditions used. For CDA, the relative K/S was improved 3.8 and 2.6 fold by cutinase-wtCBMCBHI and cutinase-sCBMCBHI, respectively, regarding cutinase alone. For treated CTA, the relative increase in K/S was not different between cutinase alone and fused to the fungal CBMs, but the initial esterase activity of cutinase was higher (figure. 7). The differences in relative K/S were also improved with the fusion of the bacterial CBM to cutinase. For CDA, cutinase-CBMN1 improved the relative K/S by 1.8 fold, the same as cutinase- PTboxCBMN1. The treatment was performed at pH 8. The optimum pH for binding of most CBMs corresponds to the optimum pH for the catalytic domain of the respective carbohydrate- active enzyme and it is in the range of acidic to neutral. The better performance on cellulose acetate fibres of the fungal CBM could be explained by the affinity of CBMCBHI to insoluble ligands being relatively more insensitive to pH than the affinity of CBMN1 (Tomme et al., 1996). In fact, lowering the treatment pH to neutral increased the adsorption of cutinase-CBMN1 to CDA (results not shown). Other reason could be the difference in size of both CBMs. The activity of cutinase could be more constrained by the bigger bacterial CBM than by the smaller fungal CBM. Indeed, using half the esterase activity in the treatment with cutinase-PTboxCBMN1, the increase in K/S obtained was in the same range of that with cutinase-CBMN1, for both fabrics (figure. 7). Further studies, aiming at a better characterization of the action of chimeric cutinases on the surface modification of cellulose acetates, would contribute to clarify these issues. 151
Subchapter 2.5 Figure 7. Protein adsorption and relative increase in K/S values for the (A) CDA and (B) CTA treated with cutinase and cutinase fused to CBMs. All the samples (1% w/v) were incubated during 18 hours with 100 U mL -1 of cutinase and cutinase-CBMN1 (cut- N1), 50 U mL -1 of cutinase-PTboxCBMN1 (cut-PT-N1) and cutinase-wtCBMT.reesei (cutwtCBM), 25 U mL -1 of cutinase-sCBMT.reesei (cut-sCBM), at pH 8 and 30º C. A control was treated under the same conditions but without any enzyme. Samples and control 152
Page 1 and 2:
Universidade do Minho Escola de Ci
Page 3 and 4:
É AUTORIZADA A REPRODUÇÃO PARCIA
Page 6:
Acknowledgments/ Agradecimentos
Page 9 and 10:
Às 2 mosqueteiras ausentes, Joana
Page 12 and 13:
Abstract The challenges facing the
Page 14 and 15:
Resumo
Page 16 and 17:
Resumo Os desafios que a indústria
Page 18 and 19:
molecular ficou retida à superfíc
Page 20 and 21:
Table of contents Acknowledgments /
Page 22 and 23:
CATs- Catalases CBD- Carbohydrate b
Page 24 and 25:
Chapter 1 General Introduction: App
Page 26 and 27:
General Introduction: Application o
Page 28 and 29:
1. Biotechnology in textile industr
Page 30 and 31:
3. Role of enzymes in textile indus
Page 32 and 33:
Page 34 and 35:
Page 36 and 37:
Page 38 and 39:
Page 40 and 41:
7. Serine proteases: subtilisins Ge
Page 42 and 43:
Page 44 and 45:
Page 46 and 47:
Page 48 and 49:
Page 50 and 51:
Page 52 and 53:
12.1 Decolourization of dyes and te
Page 54 and 55:
Page 56 and 57:
References General Introduction: Ap
Page 58 and 59:
Page 60 and 61:
Page 62 and 63:
Page 64 and 65:
Page 66 and 67:
Page 68 and 69:
Page 70 and 71:
Page 72:
Chapter 2 Surface Modification of S
Page 75 and 76:
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
Page 83 and 84:
Subchapter 2.1 60
Page 85 and 86:
Subchapter 2.2 62
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 103 and 104:
Subchapter 2.2 80
Page 105 and 106:
Subchapter 2.3 82
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
Page 119 and 120:
Subchapter 2.3 In the same set of e
Page 121 and 122:
Subchapter 2.3 98 Protein in soluti
Page 123 and 124: Subchapter 2.3 100 Protein in solut
Page 125 and 126: Subchapter 2.3 Table II. Time of wa
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 133 and 134: Subchapter 2.4 110
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 149 and 150: Subchapter 2.4 126
Page 152 and 153: Surface Modification of Cellulose A
Page 182 and 183: Chapter 3 Enzymatic Modification of
Page 184 and 185: SubChapter 3.1 Introduction
Page 186 and 187: 1. Properties of Wool Enzymatic Mod
Page 188 and 189: Enzymatic Modification of Wool Surf
Page 190 and 191: 3.3. Bleaching Enzymatic Modificati
Page 196 and 197: Subchapter 3.2 Strategies Towards t
Page 198 and 199: Strategies Towards the Functionaliz
Page 200 and 201: 1. Introduction Strategies Towards
Page 218 and 219: 4. Discussion Strategies Towards th
Page 220 and 221: References Strategies Towards the F
Page 224 and 225:
Subchapter 3.3 Enzymatic Hydolysis
Page 226 and 227:
Enzymatic Hydolysis of Wool with a
Page 228 and 229:
1. Introduction Enzymatic Hydolysis
Page 230 and 231:
Page 232 and 233:
Page 234 and 235:
Page 236 and 237:
Page 238 and 239:
References Enzymatic Hydolysis of W
Page 240 and 241:
Chapter 4 General Discussion and Fu
Page 242 and 243:
General Discussion and Future persp
Page 244 and 245:
General Discussion and Future Persp
Page 246 and 247:
References General Discussion and F
Page 248 and 249:
Appendix
Page 250 and 251:
SOB TE buffer Autoclave Tryptone 2%
Page 252:
Dissolve the nucleic acids in 30 μ
show all

Surface Modification of Cellulose Acetate with Cutinase and ...

You also want an ePaper? Increase the reach of your titles

Delete template?

Save as template?