Surface Modification of Cellulose Acetate with Cutinase and ...

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Effect of the Agitation on the Adsorption and Hydrolytic Efficiency of Cutinases on Polyethylene Terephthalate fibres (600 nm) as an average of five readings. The control samples were incubated in phosphate buffer solution. 2.6. Protein adsorption and desorption The remaining protein in the enzymatic treatment solution for different incubation periods was measured to study the adsorption and desorption phenomena (Araújo et al., 2007). For this adsorption/desorption studies the protein in solution was determined by the Bradford method using bovine serum albumin (BSA) as standard (Bradford, 1976). Different time samples of enzymatic treatment solution were measured (0, 1, 2, 3, 4 and 5 h). After 5 h of incubation, the enzymatic treatment solution was diluted (1:2) with the same previously specified phosphate buffer and the mixture was subsequent incubated for another 60 minutes, with the same agitation and temperature conditions, to verify the desorption phenomena. Values had a standard deviation below 9%. The percentage of adsorption was calculated by the following expressions as described in literature (Azevedo et al., 2000): A − B × 100 % adsorption = A D − C × 100 % desorption = A Where: A – initial protein concentration (at 0 h); B – protein concentration at time t (1, 2, 3, 4 and 5 h); C – dilution (dilution 1:2 with buffer solution); D – final protein concentration (after the dilution and 60 more minutes of incubation). 3. Results and Discussion The formation of terephthalic acid (TPA) and the protein adsorption for the two studied cutinases, with a low agitation level (shaker bath, 2A) and strong agitation level (Rotawash, 2B), is shown in figure 1. In table 1 the values of percentage of protein adsorbed for the different incubation periods are shown for both modes of mechanical agitation. (1) (2) 117
Subchapter 2.4 118 TPA (mM) TPA (mM) 0,25 0,20 0,15 0,10 0,05 0,00 0,25 0,20 0,15 0,10 0,05 0,00 Native; TPA L182A; TPA 0 1 2 3 4 5 Native without discs; TPA L182A without discs; TPA Native with discs; TPA L182A with discs; TPA A - Shaker Bath Incubation Period (h) B - Rotawash Native; Protein L182A; Protein Native without discs; Protein L182A without discs; Protein Native with discs; Protein L182A with discs; Protein 0 1 2 3 4 5 Incubation Period (h) Figure1. Terephthalic acid concentration and remaining protein concentration in the incubation liquor in a shaker bath (A) and a Rotawash machine with and without stainless steel discs (B) for different incubation periods. Initial cutinase dosed is 100 mgprotL -1 . 140 120 100 80 60 40 20 0 140 120 100 80 60 40 20 0 Protein (mgL -1 ) Protein (mgL -1 )
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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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Page 135 and 136: Subchapter 2.4 Abstract The effect
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Page 145 and 146: Subchapter 2.4 122 K/S Increase (%)
Page 147 and 148: Subchapter 2.4 References Araújo R
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3.3. Bleaching Enzymatic Modificati
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Enzymatic Modification of Wool Surf
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Enzymatic Modification of Wool Surf
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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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