2.1.8.2. Absorbency Under Load (AUL) - BADA
2.1.8.2. Absorbency Under Load (AUL) - BADA 2.1.8.2. Absorbency Under Load (AUL) - BADA
3.8.Ⅰ. Effect of Temperature Protein-based hydrogel has a high tendency to absorb the water due to hydrophilic groups. This study showed temperature plays an important role in the swelling capacity of AP hydrogel at pH 7. Figure 29 illustrates the water uptake capacity of AP hydrogel was significantly increased with temperature between 20-45 o C. Higher temperature leads to increase the diffusion of water molecules and cause the large content of water penetrates in to the polymeric network. This positive effect on the equilibrium swelling might be related to increase in the degree of expansion of the protein-based hydrogel. This hydrogel was rapidly shrunk while the temperature increased above a critical temperature (45 o C) and then water uptake was decreased. Swelling (g/g) 400 300 200 100 0 0 20 40 Temperature ( o C) Figure 29. Effect of temperature on the water uptake of AP-hydrogel 55 60
3.9.Ⅰ. Effect of Particle Size The dependency of particle size on the equilibrium swelling ratio of the EDTAD- AP hydrogel were measured by sieve analysis. The results showed that the water absorption rate was increased with decreasing particle size. Decreases in particle size caused to increases in the surface area per unit of hydrogel mass and led to rapid water absorption. Moreover the water desorption rate increased slightly with decreasing particle size for the same reason. In this study, the maximum results were obtained by use the average mesh size 25-30 for determination of swelling behavior of the AP hydrogel. 3.10.Ⅰ. FTIR-Spectroscopy analysis of AP- Superabsorbent Figure 30 shows the FT-IR spectra of unmodified albumin protein (a), EDTAD-modified AP (b) and EDTAD-AP hydrogel (c), in the frequency region from 700 to 4000 cm −1 . In spectra the broad band at 3100–3300 cm −1 due to O–H stretching, an additional peak at 2950- 3200 cm −1 occurs due to the N─H stretching of amino acids. Amide I and amide II bands illustrate two important bands of the protein infrared spectrum, so the stretching band observed at 1640 cm −1 can be attributed to amide I (RCONH2) and the peak at 1550 cm −1 is due to amide II (RCONHR') in albumin protein (Fig.30a). The EDTAD-modified protein carries carboxylate functional groups which are verified by a strong band at 1730 cm −1 (Fig.30b,30c).Moreover ,the medium band detected at 1522 cm −1 can be allocated to N-H bending coupled with C-N stretching [14] . The AP-hydrogel compared with unmodified and EDTAD-modified albumin protein indicates an important peak at 2360 cm −1 (medium), that might be due to anti-symmetric stretching ─NCO (Fig.30c), because of the rearrangement mechanism. 56
- Page 16 and 17: 1.3.1. Protein Structure Protein fo
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- Page 20 and 21: 1.3.3. Ovalbumin , Good Source for
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- Page 40 and 41: MATERIALS AND METHODS 2.1. Method o
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- Page 52 and 53: Figure 17. Schematic of device used
- Page 54 and 55: Results showed the effect of ethano
- Page 56 and 57: Preparation of protein solution (1%
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- Page 60 and 61: 3.3.Ⅰ. Effect of Buffer solution
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- Page 64 and 65: Swelling (g /g ) 350 300 250 200 15
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- Page 76 and 77: Sample Table 5. Comparison of swell
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3.9.Ⅰ. Effect of Particle Size<br />
The dependency of particle size on the equilibrium swelling ratio of the EDTAD- AP hydrogel<br />
were measured by sieve analysis. The results showed that the water absorption rate was increased<br />
with decreasing particle size. Decreases in particle size caused to increases in the surface area per<br />
unit of hydrogel mass and led to rapid water absorption. Moreover the water desorption rate<br />
increased slightly with decreasing particle size for the same reason. In this study, the maximum<br />
results were obtained by use the average mesh size 25-30 for determination of swelling behavior of<br />
the AP hydrogel.<br />
3.10.Ⅰ. FTIR-Spectroscopy analysis of AP- Superabsorbent<br />
Figure 30 shows the FT-IR spectra of unmodified albumin protein (a), EDTAD-modified AP (b)<br />
and EDTAD-AP hydrogel (c), in the frequency region from 700 to 4000 cm −1 .<br />
In spectra the broad band at 3100–3300 cm −1 due to O–H stretching, an additional peak at 2950-<br />
3200 cm −1 occurs due to the N─H stretching of amino acids. Amide I and amide II bands illustrate<br />
two important bands of the protein infrared spectrum, so the stretching band observed at 1640 cm −1<br />
can be attributed to amide I (RCONH2) and the peak at 1550 cm −1 is due to amide II (RCONHR')<br />
in albumin protein (Fig.30a).<br />
The EDTAD-modified protein carries carboxylate functional groups which are verified by a strong<br />
band at 1730 cm −1 (Fig.30b,30c).Moreover ,the medium band detected at 1522 cm −1 can be<br />
allocated to N-H bending coupled with C-N stretching [14] . The AP-hydrogel compared with<br />
unmodified and EDTAD-modified albumin protein indicates an important peak at 2360 cm −1<br />
(medium), that might be due to anti-symmetric stretching ─NCO (Fig.30c), because of the<br />
rearrangement mechanism.<br />
56