کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9675952 | 1454111 | 2005 | 5 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Comparative investigation of structure characteristics of mixed β-lactoglobulin and different chain-length phophatidylcholine monolayer at the air/water interface
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
مهندسی شیمی
شیمی کلوئیدی و سطحی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The dynamic adsorption and penetration characteristics of β-lactoglobulin into the monolayer of two different chain-length phosphatidylcholines (DSPC, DPPC) are systematically investigated using Brewster angle microscopy (BAM), fluorescence microscopy (FM) and film balance technique. It was found that all the two phosphatidylcholines can form stable complex films with the β-lactoglobulin. In the complex system of DPPC or DSPC/β-lactoglobulin the lipid domains were observed again owing to the penetration of the protein. With the increase of surface pressure, the stripe and block domains appeared and gradually turned brighter. It has been considered that protein is squeezed out from the lipid monolayer and aggregated at interface. The critical surface pressure of the β-lactoglobulin separated from DPPC or DSPC phase is increased when lipid has longer alkyl chain length. Therefore, the hydrophobic effect can be considered as a main factor to lead to the formation of a stabilized mixed lipid/protein film.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Colloids and Surfaces A: Physicochemical and Engineering Aspects - Volumes 257â258, 5 May 2005, Pages 127-131
Journal: Colloids and Surfaces A: Physicochemical and Engineering Aspects - Volumes 257â258, 5 May 2005, Pages 127-131
نویسندگان
Qiang He, Hengjian Zhang, Ying Tian, Junbai Li,