2.1.8.2. Absorbency Under Load (AUL) - BADA

More documents

Recommendations

Info

2- Side chains of polar residues with positive or negative charges, such as Arginine, Lysine, Aspartic acid and Glutamic acid are usually on the surface of the protein in contact with the aqueous solvent. 3- Uncharged polar side chains, such as Serine, Threonine, Aspargine, Glutamine, Tyrosine and Tryptophan are frequently located on the surface, but some of this are found in the interior as well as they are found in the interior, they are practically hydrogen bonded to other similar residues. In fact, hydrogen bonding helps neutralize the polarity of these groups [18] . Table 1. 22 Polar and non-polar amino acids found in proteins [18] Structure of R Amino Acid Abbreviations ─H ─CH3 ─CH(CH3) 2 ─CH2CH (CH3) 2 ─CH2CH (CH3) 2 │ CH3 ─CH2CO NH 2 ─CH2CH2CO NH 2 Glutamine Gln …………………………………………………..7 Side chain polarity Side chain charge (pH 7) Glycine Gly nonpolar neutral Alanine Ala nonpolar neutral Valine Val nonpolar neutral Leucine Leu nonpolar neutral Isoleucine Ile nonpolar neutral Phenylalanine Phe nonpolar neutral Asparagine Asn polar neutral polar negative
Complete Structure Tryptophan Trp nonpolar neutral Proline Pro nonpolar neutral ─CH2OH Serine Ser polar neutral ─CH2 OH │ CH3 Complete Structure ─CH2SH Threonine Thr polar neutral Tyrosine Tyr polar neutral Hydroxyproline Hyp nonpolar neutral Cysteine Cys nonpolar neutral ─CH2S │ Cystine Cys-Cys nonpolar neutral ─CH2S ─CH2CH2SCH3 ─CH2COOH ─CH2CH2CH2CH2NH2 ─CH2CH2CH2NH─C─NH2 Methionine Met nonpolar neutral Aspartic acid Asp polar negative Lysine Lys polar positive NH ║ Arginine Arg polar positive ……………………………………………………8 Histidine His polar positive
Page 2 and 3: BIOSUPERABSORBENT FROM PROTEINS Sar
Page 4 and 5: ACKNOWLEDGMENTS We would like to ap
Page 6 and 7: CONTENTS ACKNOWLEDGMENTS ………
Page 8 and 9: 3.4.Ⅰ. Kinetic of Swelling……
Page 10 and 11: 22- Effect of Glutaraldehyde concen
Page 12 and 13: 1 INTRODUCTION Superabsorbent hydro
Page 14 and 15: 1.1. Definition of Superabsorbency
Page 16 and 17: 1.3.1. Protein Structure Protein fo
Page 20 and 21: 1.3.3. Ovalbumin , Good Source for
Page 22 and 23: One of the paper preparation proces
Page 24 and 25: ……………………………
Page 26 and 27: 1.5. The Thermodynamic of Protein F
Page 28 and 29: In order to chemical modification o
Page 30 and 31: The swollen crosslinked polymer may
Page 32 and 33: 1.7.1.3. Crosslinking by UV-Irradia
Page 34 and 35: 1.7.2.1. Non-specific Crosslinking
Page 36 and 37: 1.8. Determination the Degree of cr
Page 38 and 39: These preparations contain consider
Page 40 and 41: MATERIALS AND METHODS 2.1. Method o
Page 42 and 43: ased on the solubility of the prote
Page 44 and 45: 2.1.2.2. Determination of Zygomycet
Page 46 and 47: 2.1.3. Modification of proteins Alb
Page 48 and 49: The first step was weighted a 30 mg
Page 50 and 51: 2.1.8.1. Centrifuge Retention Capac
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%
Page 58 and 59: PART Ⅰ ALBUMIN SUPERABSORBENT HYD
Page 60 and 61: 3.3.Ⅰ. Effect of Buffer solution
Page 62 and 63: Swelling (g/g) 300 200 100 0 1 0.01
Page 64 and 65: Swelling (g /g ) 350 300 250 200 15
Page 66 and 67: 3.8.Ⅰ. Effect of Temperature Prot
Page 68 and 69:
In this rearrangement the R─ grou
Page 70 and 71:
Calculations As a result by solving
Page 72 and 73:
In the present work, increasing the
Page 74 and 75:
In detail, Figure 36 shows the comp
Page 76 and 77:
Sample Table 5. Comparison of swell
Page 78 and 79:
The IZP-hydrogel compared with unmo
Page 80 and 81:
According to our results, the swell
Page 82 and 83:
REFERENCES 1- Fredric L.Buchholz &
Page 84 and 85:
32- Alexander,. J, Colloid chemistr
show all

2.1.8.2. Absorbency Under Load (AUL) - BADA

Create successful ePaper yourself

Delete template?

Save as template?