Effects of enzymatic modifications and botanical source on starch-stearic acid complex formation

2016 ◽  
Vol 68 (7-8) ◽  
pp. 700-708 ◽  
Author(s):  
Emily Oluwaseun Arijaje ◽  
Ya-Jane Wang
Keyword(s):  
Complex Formation ◽  
Stearic Acid ◽  
Acid Complex

Effects of Chemical and Enzymatic Modifications on Starch–Stearic Acid Complex Formation

2014 ◽  
Vol 62 (13) ◽  
pp. 2963-2972 ◽  
Author(s):  
Emily Oluwaseun Arijaje ◽  
Ya-Jane Wang ◽  
Sara Shinn ◽  
Utkarsh Shah ◽  
Andrew Proctor
Keyword(s):  
Complex Formation ◽  
Stearic Acid ◽  
Acid Complex

Sorption of α-amino-acids by copper montmorillonite

Clay Minerals ◽  
1967 ◽  
Vol 7 (2) ◽  
pp. 167-176 ◽  
Author(s):  
W. Bodenheimer ◽  
L. Heller
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Complex Formation ◽  
Glutamic Acid ◽  
Acid Complex ◽  
X Ray ◽  
Ray Methods

AbstractSorption of an acidic, amphoteric, sulphur containing and basic α-amino-acid (glutamic acid, glycine, methionine and lysine) by copper montmorillonite was studied by chemical and X-ray methods. With glutamic acid complex formation occurs only in solution but increasing basicity of the aminoacid favours complex formation in the clay interlayers.

scholarly journals Morphology, pasting and thermal properties of microwave-assisted cassava starch- stearic acid complex

2020 ◽  
Vol 49 (3) ◽  
pp. 275
Author(s):  
S. A. Oyeyinka ◽  
T. M. Afunso ◽  
A. A. Adeloye ◽  
S. S. Diarra
Keyword(s):  
Thermal Properties ◽  
Stearic Acid ◽  
Cassava Starch ◽  
Acid Complex ◽  
Microwave Assisted

scholarly journals Zeta Potential and Turbidimetry Analyzes for the Evaluation of Chitosan/Phytic Acid Complex Formation

2014 ◽  
Vol 3 (2) ◽  
pp. 71 ◽  
Author(s):  
Noura Saïed ◽  
Mohammed Aider
Keyword(s):  
Acetic Acid ◽  
Complex Formation ◽  
Zeta Potential ◽  
Acid Solution ◽  
Surface Charge ◽  
Phytic Acid ◽  
Acetic Acid Solution ◽  
Deionized Water ◽  
Acid Complex ◽  
Ph Range

<p>The aim of this work was to study the possible complex formation between chitosan and phytic acid. Zeta potential and turbidity measurements were used as a basis to confirm the possible complex between these two molecules. The obtained results showed that chitosan at a concentration of 0.1% (w/v) were soluble in 0.1% acetic acid solution. This concentration of the acetic acid was the lowest that allows chitosan to dissolve. A positive surface charge of chitosan was recorded in the pH interval from 1 to 7. The highest zeta potential values were obtained at pH &lt; 5 and decreased significantly at pH 6 and 7. Regarding phytic acid, it was soluble in deionized water and acetic acid whatever the concentration of the acetic acid and in the entire pH range 2-10. Phytic acid had negative surface charge in deionized water and in 0.1% acetic acid, but was slightly positively charged in 5% acetic acid solution. The solubility of chitosan was decreased by the presence of phytic acid. The formation of chitosan/phytic acid complex as monitored by measuring the zeta potential does not allow us to conclude that the formation of this complex is possible.</p>

Evidence for albumin – Cu(II) – amino acid ternary complex

1968 ◽  
Vol 46 (6) ◽  
pp. 601-607 ◽  
Author(s):  
Bibudhendra Sarkar ◽  
Yuk Wigfield
Keyword(s):  
Amino Acid ◽  
Human Serum Albumin ◽  
Complex Formation ◽  
Binding Sites ◽  
Ternary Complex ◽  
Binding Studies ◽  
Acid Complex ◽  
Ternary Complex Formation ◽  
Chelex 100 ◽  
Amino Acid Complex

Commercially obtained pure human serum albumin (HSA) was shown to contain molecular aggregates and was significantly contaminated with Cu(II). A solution of commercial HSA was first passed through a Sephadex G-200 column to obtain pure monomeric HSA. The monomer of HSA was subsequently passed through Chelex-100 resin to free it from Cu(II). All Cu(II)-binding studies were conducted with monomeric and copper-free HSA. The first Cu(II)-binding site on HSA appears to be stronger than the second and the subsequent binding sites. Significant amounts of L-histidine and L-threonine were bound to HSA when Cu(II) was added in the form of Cu(II) – amino acid complexes. In the absence of Cu(II), free L-histidine or L-threonine do not bind to HSA at pH 7.4. It is concluded that, in the presence of either L-histidine or L-threonine, ternary complex formation is involved both at the first and the subsequent binding sites for Cu(II) on HSA. In view of this finding, it appears that the equilibrium between HSA–Cu(II) and Cu(II) – amino acid complex is mediated through a ternary complex HSA – Cu(II) – amino acid.

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