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IN VITRO DIGESTIBILITY OF CHINESE TARTARY BUCKWHEAT PROTEIN FRACTIONS: THE MICROSTRUCTURE AND MOLECULAR WEIGHT DISTRIBUTION OF THEIR HYDROLYSATES
Author(s) -
GUO XIAONA,
YAO HUIYUAN,
CHEN ZHENGXING
Publication year - 2006
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.2006.00078.x
Subject(s) - glutelin , prolamin , hydrolysate , pepsin , chemistry , globulin , chromatography , albumin , food science , digestion (alchemy) , biochemistry , storage protein , enzyme , biology , hydrolysis , immunology , gene
Our previous study showed that in vitro pepsin digestibility of Chinese tartary buckwheat protein was relatively low compared to those of other edible seeds. In vitro pepsin digestibilities of four protein fractions of tartary buckwheat, microstructure and molecular weight (MW) distributions of hydrolysates were investigated. In vitro pepsin digestion assay showed that the digestibilities of tartary buckwheat protein fractions were albumin (81.20%), globulin (79.56%), prolamin (66.99%) and glutelin (58.09%). Scanning electron microscopy showed that albumin and globulin fractions were digested by pitting from the outer surface to the inner part and were more digestible, while prolamin and glutelin fractions resisted digestion because only the outer surfaces of their protein bodies were digested and the interior was protected. MW distribution of the hydrolysates from the four protein fractions was determined by high‐performance liquid chromatography. The hydrolysates of albumin mainly consisted of polypeptides with lower MW. The hydrolysates of glutelin had larger polypeptides together with small and medium‐sized peptide fractions.