Relationship of Structure to Properties of Some Anionic Surfactants as Collectors in the Flotation Process. 1. Effect of Chain Length

1999 ◽  
Vol 44 (1) ◽  
pp. 133-137 ◽  
Author(s):  
N. A. Abdel-Khalek ◽  
A. M. A. Omar ◽  
Y. Barakat
Biologia ◽  
2008 ◽  
Vol 63 (6) ◽  
Author(s):  
Wataru Saburi ◽  
Hironori Hondoh ◽  
Young-Min Kim ◽  
Haruhide Mori ◽  
Masayuki Okuyama ◽  
...  

AbstractDextran glucosidase from Streptococcus mutans (SMDG), an exo-type glucosidase of glycoside hydrolase (GH) family 13, specifically hydrolyzes an α-1,6-glucosidic linkage at the non-reducing ends of isomaltooligosaccharides and dextran. SMDG shows the highest sequence similarity to oligo-1,6-glucosidases (O16Gs) among GH family 13 enzymes, but these enzymes are obviously different in terms of substrate chain length specificity. SMDG efficiently hydrolyzes both short-and long-chain substrates, while O16G acts on only short-chain substrates. We focused on this difference in substrate specificity between SMDG and O16G, and elucidated the structure-function relationship of substrate chain length specificity in SMDG. Crystal structure analysis revealed that SMDG consists of three domains, A, B, and C, which are commonly found in other GH family 13 enzymes. The structural comparison between SMDG and O16G from Bacillus cereus indicated that Trp238, spanning subsites +1 and +2, and short β → α loop 4, are characteristic of SMDG, and these structural elements are predicted to be important for high activity toward long-chain substrates. The substrate size preference of SMDG was kinetically analyzed using two mutants: (i) Trp238 was replaced by a smaller amino acid, alanine, asparagine or proline; and (ii) short β → α loop 4 was exchanged with the corresponding loop of O16G. Mutant enzymes showed lower preference for long-chain substrates than wild-type enzyme, indicating that these structural elements are essential for the high activity toward long-chain substrates, as implied by structural analysis.


2014 ◽  
Vol 63 (10) ◽  
pp. 995-1004 ◽  
Author(s):  
Fumiko Yamaguchi ◽  
Shin-ichi Watanabe ◽  
Fusae Harada ◽  
Miyuki Miyake ◽  
Masaki Yoshida ◽  
...  

1992 ◽  
Vol 62 (3) ◽  
pp. 140-143 ◽  
Author(s):  
L. A. Holt ◽  
J. S. Kelson ◽  
R. N. Reddie

Wool samples containing various anionic surfactants (alkylbenzene sulphonates, primary and secondary alkane sulphonates, and an olefin sulphonate) lose some of the surfactant to the treatment liquor when subjected to typical dyeing conditions. At the boil, equilibrium is set up within 15 minutes between the concentration of surfactant in the liquor and that on the fiber. The extent of extraction is influenced by the alkyl chain length of the surfactant, the pH of the liquor, and the bath volume. For many surfactants, less than 5% is extracted at a 20:1 liquor/wool ratio in the pH range 5–6. The presence of nonionic surfactant in the treatment liquors results in slightly higher levels of extraction. Exhaustion of anionic surfactants onto wool gives distributions of surfactant between the wool and liquor similar to those obtained when treated wools are extracted under the same conditions of temperature, pH, and liquor/wool ratio.


2011 ◽  
Vol 364 (2) ◽  
pp. 395-399 ◽  
Author(s):  
Arnab Maity ◽  
Prasun Ghosh ◽  
Tarasankar Das ◽  
Jyotirmayee Dash ◽  
Pradipta Purkayastha

2001 ◽  
Vol 9 (2) ◽  
pp. 487-492 ◽  
Author(s):  
Masaaki Ueki ◽  
Shigeru Watanabe ◽  
Takeshi Saitoh ◽  
Hideki Nakashima ◽  
Naoki Yamamoto ◽  
...  

2008 ◽  
Vol 61 (2) ◽  
pp. 98-102 ◽  
Author(s):  
Ikuko Kozone ◽  
Makoto Hashimoto ◽  
Udo Gräfe ◽  
Hiroshi Kawaide ◽  
Hiroshi Abe ◽  
...  

1985 ◽  
Vol 19 (11) ◽  
pp. 797-802 ◽  
Author(s):  
B. V. Passet ◽  
A. A. Golubyatnikova ◽  
N. V. Enina ◽  
S. V. Nekrasov ◽  
E. T. Mordvinova

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