The molecular size reduction and the formation of bitterness during a tryptic hydrolysis of soybean 11S glycinin were determined by using quantitative analysis and organoleptic evaluation. The 11S glycinin of 90% purity was prepared by cryoprecipitation and Con A Sepharose 4B affinity chromatography, and hydrolyzed with trypsin in a pH-stat reactor for 4h. Bitterness was formed within 1 h of hydrolysis, and then slowly increased up to 3.5x10-5M quinine-HCl equivalent. The extent of hydrolysis (DH) was 7% at 1 h and increased up to 12% by the end of the reaction. The α-amino nitrogen content increased from an initial 0.7 mM to 7 mM at the end of the period. The SDS-PAGE analysis showed that the acidic subunit of 11S glycinin was mostly hydrolyzed. The GP-HPLC analysis indicated that the bitterness was mainly contributed by the peptide fractions of molecular weights of 360- 2,100 Da.
|Number of pages||5|
|Journal||Journal of microbiology and biotechnology|
|Publication status||Published - 1999 Aug|
- Enzymatic hydrolysis
- Soybean protein
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology