Insoluble gluten was solubilized by proteases (chymotrypsin, papain,
Pronase, and pepsin) or mild
acid (0.05 N HCl) treatments. The digests and hydrolysate are
turbid, but after transglutaminase
(TGase) treatment, the turbid mixture was converted to a transparent
solution, which was found to
be soluble at a wide range of pH. The hydrophobicity was greatly
decreased after polymerization
by TGase. SDS−PAGE patterns of the digests and hydrolysate with
and without TGase treatment
showed that the digests (except Pronase) were polymerized by TGase.
The emulsifying properties
of the polymerized peptides were greatly improved compared to those of
the protease digests and
acid hydrolysates. The foaming properties of the polymerized
digests were also greatly improved.
The digests and hydrolysate were found to have a bitter taste, but
after polymerization the bitterness
completely disappeared.
Keywords: Functional properties; gluten; protease; hydrolysis; microbial
transglutaminase
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