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- W2389811597 abstract "The use of cycledextrin as host to provide a special environment for organic reactions and for enzyme models has received considerable attention in recent years. However, in cyclodextrin both the size and length of the hydrophobic cavity are fixed. In this paper, another type of inclusion with sodium carboxymethylamylose (Na-CMA) playing the role of the host which provides a cavity with the characteristics similar to that of cyclodextrin but with more flexibility in its size and length was described. The substrates with hydrophobic long hydrocarbon chain used were: cetyltrimethylammonium chloride (CTACl); lauryltrimethylammonium iodide (LTAI) and sodium laurylsulfate (NaLS).Intrinsic association constant (K_A~*) determined by surface tension-concentration of substrate curves are about 1.27～2.30×10~4 M~(-1) within the range of temperature and Na-CMA concentration studied for Na-CMA—CTACl system, 0.73×10~3 M~(-1) for Na-CMA—NaLS and 0.52×10~3 M~(-1) for Na-CMA—LTAI respectively. Based on data derived from 6-helix conformation of Na-CMA and relative molecular length of various substrates, the calculated number of binding site n are 7.1, 9.4 and 9.8, whereas experimental results are 7.7, 10 and 9.8, for CTACl, NaLS and LTAI respectively.From the temperature dependence of K_A~*, the following values of thermodynamic parameters were obtained: ⊿G_(298)=-5.7 kcal/mole, AH=-3.5 kcal/mole, ⊿S_(298)= 7.6 e. u. for the Na-CMA—CTACl system. This results indicates that the driving force for the inclusion process here is different from either the typically entropy-controlled hydrophobic interaction or the enthalpy-controllod mechanism of cyclodextrin inclusion.The above observations together with results from viscometry and surface activity experiments suggest that the inclusion process involves the change of existing extended coil conformation to interrupted helix. Possibly the helical conformation of amylose and its derivatives may serve as a better model for enzymes than cyclodextrin." @default.
- W2389811597 created "2016-06-24" @default.
- W2389811597 creator A5052315803 @default.
- W2389811597 date "1981-01-01" @default.
- W2389811597 modified "2023-09-25" @default.
- W2389811597 title "THE MICROENVIRONMENTAL EFFECTS OF THE HELICAL CONFORMATIONS OF AMYLOSE AND ITS DERIVATIVES 1. THE INCLUSION OF THE SUBSTRATES CARRYING A HYDROPHOBIC LONG HYDROCARBON CHAIN WITH SODIUM CARBOXYMETHYLAMYLOSE AS THE HOST" @default.
- W2389811597 hasPublicationYear "1981" @default.
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