Browsing by Subject "Oat proteins"

Oat protein is a valuable cereal protein with high protein content and a good balance of amino acids profile. However, the inflexible molecular structure and poor watersolubility of oat protein limit its application in food industry. To exploit the food use of oat, the functionalities of oat proteins should be improved. ?-chymotrypsin, a proteolytic enzyme, has been proven as being able to deamidate some food proteins without severe hydrolysis under alkaline pH conditions, hence to improve the protein functionalities. The aim of this research was to test whether oat protein could be deamidated by ?- chymotrypsin under alkaline pH conditions. The extent of ?-chymotrypsin-induced proteolysis on oat protein was also studied. Oat protein was treated by ?-chymotrypsin under alkaline conditions from pH 8 to 11 at room temperature for 2 hours. The deamidation degrees of the proteins were measured by ammonia quantification. The hydrolysis degrees of proteins were analyzed by trichloroacetic acid precipitation and protein quantification method. The changes of molecular weights were analyzed by SDS-PAGE and SE-HPLC. The action of ?-chymotrypsin under alkaline pH conditions induced slight deamidation of oat protein to low deamidation degrees (9-12%). On the other hand, ?-chymotrypsin mainly caused hydrolysis of oat protein to hydrolysis degrees between 49% and 62%. SDS-PAGE and SE-HPLC analysis also revealed that significant hydrolysis of oat protein occurred during the reaction. The hydrolysis mainly caused the shift of oat protein fractions from molecular weight above 20 kDa to molecular weight below 15 kDa. Change in pH did not cause significant differences on deamidation degrees and hydrolysis degrees of oat protein In conclusion, oat protein could not be effectively deamidated by ?-chymotrypsin under alkaline pH conditions, while the proteolysis was severe.