TY - JOUR
T1 - Optimal condition to remove mercury in yellowfin tuna protein isolates and ACE-inhibitory property of peptide prepared using commercial proteases
AU - Kokkaew, Hathaigan
AU - Thawornchinsombut, Supawan
AU - Park, Jae Won
N1 - Publisher Copyright:
© 2009 RDO All Rights Reserved.
PY - 2016
Y1 - 2016
N2 - Response surface methodology (RSM) was performed to maximize the mercury (Hg) reduction from yellowfin tuna (Thunnus albacare) by products protein isolates (YBPI). The optimal condition of Hg reduction (89.3%) was 10.5 mM CaCl2 and a Water:YB of 12.9:1, while other variables were fixed at 5 mM citric acid, 60 min incubation, pH 11 and 8,000 x g for 15 min of centrifugation. At these conditions, the significant protein recovery (80.1%) was obtained. Hydrolysates sequentially hydrolyzed with G6 followed by GN exhibited the highest angiotensin I-converting enzyme (ACE) inhibitory activity than other enzyme preparations. Fractionated yellowfin tuna by products protein hydrolysate (YBPH) increased in ACE-inhibitory activity when peptide size decreased. In-vitro gastrointestinal (GI) digestion significantly increased bioactive property. ACEinhibitory activity of YBPH with and without simulated GI digestion significantly increased after incubating against ACE, demonstrating pro-drug type peptides.
AB - Response surface methodology (RSM) was performed to maximize the mercury (Hg) reduction from yellowfin tuna (Thunnus albacare) by products protein isolates (YBPI). The optimal condition of Hg reduction (89.3%) was 10.5 mM CaCl2 and a Water:YB of 12.9:1, while other variables were fixed at 5 mM citric acid, 60 min incubation, pH 11 and 8,000 x g for 15 min of centrifugation. At these conditions, the significant protein recovery (80.1%) was obtained. Hydrolysates sequentially hydrolyzed with G6 followed by GN exhibited the highest angiotensin I-converting enzyme (ACE) inhibitory activity than other enzyme preparations. Fractionated yellowfin tuna by products protein hydrolysate (YBPH) increased in ACE-inhibitory activity when peptide size decreased. In-vitro gastrointestinal (GI) digestion significantly increased bioactive property. ACEinhibitory activity of YBPH with and without simulated GI digestion significantly increased after incubating against ACE, demonstrating pro-drug type peptides.
KW - Commercial enzymes
KW - Gastrointestinal digestion
KW - Pro-drug type peptides
KW - Response surface methodology
UR - http://www.scopus.com/inward/record.url?scp=84985998530&partnerID=8YFLogxK
M3 - Article
AN - SCOPUS:84985998530
SN - 0125-3395
VL - 38
SP - 439
EP - 447
JO - Songklanakarin Journal of Science and Technology
JF - Songklanakarin Journal of Science and Technology
IS - 4
ER -