Analysis of Protein Moiety of Polysaccharide Conjugates Water-extracted from Low Grade Green Tea

Tea polysaccharide conjugates(TPCs) were water-extracted and purified from low-grade green tea. Al-though TPC contains 1.97% covalent binding proteins, Coomassie brilliant blue G250 and R250 could not detect this protein. The "should-shape" absorption peak observed at 250–280 nm in the UV-...

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Published inChemical research in Chinese universities Vol. 34; no. 4; pp. 691 - 696
Main Authors Chen, Xiaoqiang, Shao, Shengrong, Xie, Jianchun, Yuan, Hao, Li, Qian, Wu, Long, Wu, Zhengqi, Yuan, Haibo, Jiang, Yongwen
Format Journal Article
LanguageEnglish
Published Changchun Jilin University and The Editorial Department of Chemical Research in Chinese Universities 01.08.2018
Springer Nature B.V
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Summary:Tea polysaccharide conjugates(TPCs) were water-extracted and purified from low-grade green tea. Al-though TPC contains 1.97% covalent binding proteins, Coomassie brilliant blue G250 and R250 could not detect this protein. The "should-shape" absorption peak observed at 250–280 nm in the UV-Vis spectrum was caused by quinone compounds derived from polyphenol oxidation during TPC extraction. The UV-Vis spectrum could be used to detect the decolorizing degree of TPC. TPC aqueous solution merely presented the negative charge properties of its polysaccharides instead of the acid-base property of its protein section, and exhibited higher stability at pH greater than 5.0. No precipitation or haze occurred in three TPC/epigallocatechin gallate(EGCG) aqueous mixtures during 12 h storage. TPC had emulsifying activity, which indicated that its protein moiety formed hydrophobic groups. It is proposed that some of the physicochemical properties of the TPC protein moiety are shielded by its polysaccharide chain.
ISSN:1005-9040
2210-3171
DOI:10.1007/s40242-018-7335-7