Characterization of hydrolysates derived from enzymatic hydrolysis of wheat gluten.
The aim of this study is to investigate the characteristics of wheat gluten hydrolysates. Enzymatic hydrolysis was performed using a papain (food-grade enzyme) in the present study. The gluten proteins were hydrolyzed for 8 h. During enzymatic hydrolysis, average peptide chain length in the hydrolysate decreased rapidly. Increasing proteolysis resulted in the increase in the contents of the soluble forms of nitrogen. However, the content of peptide nitrogen increased within the 1st 6 h, and then began to decrease. The percentage of the released peptides with molecular weight (MW) of over 15 kD decreased with extending enzymatic hydrolysis, while those with MW below 5 kD increased significantly (P < 0.05). The peptides with MW 10 to 15 kD and those having the MW 5 to 10 kD had different changes. The polymeric glutenin and monomeric gliadin in gluten complex showed different behavior after enzymatic hydrolysis. The monomeric protein (gliadin) and soluble glutenin were prone to enzymatic hydrolysis, while insoluble glutenin was resistance to enzymatic hydrolysis.
Wang
Jin-Shui
JS
College of Light Industry and Food Science, South China Univ. of Technology, Guangzhou 510640, People's Republic of China.
Zhao
Mou-Ming
MM
Zhao
Qiang-Zhong
QZ
Bao
Yang
Y
Jiang
Yue-Ming
YM
D005524:Food Technology; D005903:Gliadin / Q000737:chemistry / Q000378:metabolism; D005983:Glutens / Q000737:chemistry* / Q000378:metabolism*; D006868:Hydrolysis; D008970:Molecular Weight; D009584:Nitrogen / Q000378:metabolism; D010206:Papain / Q000378:metabolism*; D010316:Particle Size; D010446:Peptide Fragments / Q000378:metabolism; D012995:Solubility; D013997:Time Factors; D014908:Triticum / Q000737:chemistry*
D010446:Peptide Fragments; D005983:Glutens; D005903:Gliadin; D010206:Papain; C037302:glutenin; D009584:Nitrogen