Integrated Evaluation of Dual-Functional DPP-IV and ACE Inhibitory Effects of Peptides Derived from Sericin Hydrolysis and Their Stabilities during In Vitro-Simulated Gastrointestinal and Plasmin Digestions

被引:8
|
作者
Sangsawad, Papungkorn [1 ]
Katemala, Sasikan [2 ]
Pao, Danou [3 ]
Suwanangul, Saranya [4 ]
Jeencham, Rachasit [3 ]
Sutheerawattananonda, Manote [3 ]
机构
[1] Suranaree Univ Technol, Inst Agr Technol, Sch Anim Technol & Innovat, Nakhon Ratchasima 30000, Thailand
[2] Kasetsart Univ, Fac Agr, Dept Anim Sci Agr Bioresources & Food, Kamphaeng Saen Campus, Nakhon Pathom 73140, Thailand
[3] Suranaree Univ Technol, Inst Agr Technol, Sch Food Technol, Nakhon Ratchasima 30000, Thailand
[4] Maejo Univ, Fac Engn & Agroind, Program Food Sci & Technol, Chiang Mai 50290, Thailand
关键词
sericin; bioactive peptide; ACE; DPP-IV; gastrointestinal digestion; IN-VITRO; SILK SERICIN; PROTEIN; FOOD;
D O I
10.3390/foods11233931
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Sericin, a byproduct of the silk industry, is an underutilized protein derived from the yellow silk cocoon. This research aimed to produce and characterize the bioactive peptides from sericin using various enzymatic hydrolysis methods. Alcalase, papain, neutrase, and protease were tested under their respective digestion conditions. Among the enzymes tested, neutrase-catalyzed sericin into specific peptides with the strongest dipeptidyl peptidase IV (DPP-IV) and angiotensin-converting enzyme (ACE) inhibitory properties. The peptides were subjected to a simulated in vitro gastrointestinal (GI) digestion in order to determine their stability. The GI peptides that were produced by neutrase hydrolysis continued to have the highest DPP-IV and ACE inhibitory activities. The neutrase -digested peptides were then fractionated via ultrafiltration; the peptide fraction with a molecular weight <3 kDa (UF3) inhibited DPP-IV and ACE activities. After being subjected to in vitro blood plasma hydrolysis, the UF3 was slightly degraded but retained its bioactivity. As a result of these findings, sericin peptides can be utilized as novel dietary ingredients that may alleviate some metabolic syndromes via the dual inhibitory properties of DPP-IV and ACE.
引用
收藏
页数:13
相关论文
共 2 条
  • [1] In silico identification of novel ACE and DPP-IV inhibitory peptides derived from buffalo milk proteins and evaluation of their inhibitory mechanisms
    Gu, Yuxiang
    Li, Xing
    Qi, Xiaofen
    Ma, Ying
    Chan, Eric Chun Yong
    AMINO ACIDS, 2023, 55 (02) : 161 - 171
  • [2] In silico identification of novel ACE and DPP-IV inhibitory peptides derived from buffalo milk proteins and evaluation of their inhibitory mechanisms
    Yuxiang Gu
    Xing Li
    Xiaofen Qi
    Ying Ma
    Eric Chun Yong Chan
    Amino Acids, 2023, 55 : 161 - 171