Premium
HYPOTENSIVE ACTIVITY OF MUSCLE PROTEIN AND GLUTEN HYDROLYSATES OBTAINED BY PROTEASE TREATMENT
Author(s) -
SAIGA AI,
KANDA KEIKO,
WEI ZHENG,
OKUMURA TOMOYUKI,
KANEKO TOSHIYUKI,
NISHIMURA TOSHIHIDE
Publication year - 2002
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.1745-4514.2002.tb00761.x
Subject(s) - hydrolysate , papain , chemistry , trypsin , gluten , myofibril , molecular mass , protease , ic50 , pharmacology , chymotrypsin , biochemistry , enzyme , chromatography , food science , hydrolysis , medicine , in vitro
Protein hydrolysates obtained by treatment with papain, trypsin, chymotrypsin and actinase all exhibited inhibitory activity (IC50: 3.4–41.8 mg%) toward angiotensin‐converting enzyme (ACE) (EC 3.4.15.1). In particular, the protein hydrolysate obtained by treatment with papain showed the highest inhibitory activity (3.7–5.3 mg%). The ACE inhibitory activity of the gluten hydrolysate obtained with actinase was mainly due to peptides of less than 500 Da in molecular mass. On the other hand, the ACE inhibitory activity of the myofibrillar protein hydrolysate obtained with papain was due to peptides of both less and more than 500 Da in molecular mass. The blood pressure of spontaneously hypertensive rats (SHR) administered the myofibrillar protein hydrolysate was significantly reduced at 2 h after administration. The blood pressure of SHR was also reduced at 2 h after administration of the gluten hydrolysate, and this effect continued until 6 h. These hydrolysates may potentially be useful as antihypertensive food materials .