Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide
Polysaccharide conjugates were alkali-extracted from green tea (TPC-A). Although it contained 11.80% covalently binding proteins, TPC-A could not bind to the Coomassie Brilliant Blue dyes G250 and R250. TPC-A had no expected characteristic absorption peak of protein in the UV-vis spectrum scanning i...
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doaj-25fd817c04564650a04b38a9281329dd2020-11-25T00:16:53ZengMDPI AGMolecules1420-30492017-05-0122691410.3390/molecules22060914molecules22060914Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its PolysaccharideXiaoqiang Chen0Wei Song1Jin Zhao2Zhifa Zhang3Yuntian Zhang4College of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, ChinaDepartment of Food Science and Engineering, MIITKey Laboratory of Critical Materials Technology for New Energy Conversion and Storage, School of Chemistry and Chemical Engineering, Harbin Institute of Technology, Harbin 150090, ChinaCollege of Life Science, China Jiliang University, Hangzhou 310018, ChinaTongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, ChinaCollege of Bioengineering and Food, Hubei University of Technology, Wuhan 430068, ChinaPolysaccharide conjugates were alkali-extracted from green tea (TPC-A). Although it contained 11.80% covalently binding proteins, TPC-A could not bind to the Coomassie Brilliant Blue dyes G250 and R250. TPC-A had no expected characteristic absorption peak of protein in the UV-vis spectrum scanning in the range of 200–700 nm. The UV-vis wavelength of 280 nm was not suitable to detect the presence of the protein portion of TPC-A. The zeta potential of TPC-A merely presented the negative charge properties of polysaccharides instead of the acid–base property of its protein section across the entire pH range. Furthermore, TPC-A was more stable when the pH of solution exceeded 4.0. In addition, no precipitation or haze was generated in the TPC-A/(−)-epigallocatechin gallate (EGCG) mixtures during 12 h storage. TPC-A has emulsifying activity, which indicated that its protein moiety formed hydrophobic groups. Thus, it was proposed that some physical properties of TPC-A protein were shielded by its olysaccharide, since the protein moiety was wrapped by its polysaccharide chains.http://www.mdpi.com/1420-3049/22/6/914alkali-extractedtea polysaccharide conjugatesprotein |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Xiaoqiang Chen Wei Song Jin Zhao Zhifa Zhang Yuntian Zhang |
spellingShingle |
Xiaoqiang Chen Wei Song Jin Zhao Zhifa Zhang Yuntian Zhang Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide Molecules alkali-extracted tea polysaccharide conjugates protein |
author_facet |
Xiaoqiang Chen Wei Song Jin Zhao Zhifa Zhang Yuntian Zhang |
author_sort |
Xiaoqiang Chen |
title |
Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide |
title_short |
Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide |
title_full |
Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide |
title_fullStr |
Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide |
title_full_unstemmed |
Some Physical Properties of Protein Moiety of Alkali-Extracted Tea Polysaccharide Conjugates Were Shielded by Its Polysaccharide |
title_sort |
some physical properties of protein moiety of alkali-extracted tea polysaccharide conjugates were shielded by its polysaccharide |
publisher |
MDPI AG |
series |
Molecules |
issn |
1420-3049 |
publishDate |
2017-05-01 |
description |
Polysaccharide conjugates were alkali-extracted from green tea (TPC-A). Although it contained 11.80% covalently binding proteins, TPC-A could not bind to the Coomassie Brilliant Blue dyes G250 and R250. TPC-A had no expected characteristic absorption peak of protein in the UV-vis spectrum scanning in the range of 200–700 nm. The UV-vis wavelength of 280 nm was not suitable to detect the presence of the protein portion of TPC-A. The zeta potential of TPC-A merely presented the negative charge properties of polysaccharides instead of the acid–base property of its protein section across the entire pH range. Furthermore, TPC-A was more stable when the pH of solution exceeded 4.0. In addition, no precipitation or haze was generated in the TPC-A/(−)-epigallocatechin gallate (EGCG) mixtures during 12 h storage. TPC-A has emulsifying activity, which indicated that its protein moiety formed hydrophobic groups. Thus, it was proposed that some physical properties of TPC-A protein were shielded by its olysaccharide, since the protein moiety was wrapped by its polysaccharide chains. |
topic |
alkali-extracted tea polysaccharide conjugates protein |
url |
http://www.mdpi.com/1420-3049/22/6/914 |
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