Production of ACE inhibitory peptides from sweet sorghum grain protein using alcalase: Hydrolysis kinetic, purification and molecular docking study

文献类型： 外文期刊

第一作者： Wu, Qiongying

作者： Wu, Qiongying;Du, Jinjuan;Jia, Junqiang;Kuang, Cong;Wu, Qiongying;Jia, Junqiang

作者机构：

关键词： Sweet sorghum;Hydrolysis kinetic;ACE inhibitory peptide;Purification;Molecular docking

期刊名称：FOOD CHEMISTRY （ 影响因子：7.514； 五年影响因子：7.516 ）

ISSN：

年卷期：

页码：

收录情况： SCI

摘要： In this study, sweet sorghum grain protein (SSGP) was hydrolyzed using alcalase yielding ACE inhibitory peptides. A kinetic model was proposed to describe the enzymolysis process of SSGP. The kinetic parameters, a and b, were determined according to experimental data. It was found that the model was reliable to describe the kinetic behaviour for SSGP hydrolysis by alcalase. After hydrolysis, the SSGP hydrolysate with DH of 19% exhibited the strongest ACE inhibitory activity and the hydrolysate was then used to isolate ACE inhibitory peptides. A novel ACE inhibitory peptide was successfully purified from this hydrolysate by ultrafiltration, ion exchange chromatography, gel filtration chromatography, and reversed-phased high performance liquid chromatography (RP-HPLC). The amino acid sequence of the purified peptide was identified as Thr-Leu-Ser (IC(5)0 = 102.1 mu M). The molecular docking studies revealed that the ACE inhibition of the tripeptide was mainly attributed to its C-terminal Ser, which can effectively interact with the S1 and S2 pockets of ACE. Our studies suggest that the tripeptide from the SSGP hydrolysate can be utilized to develop functional food ingredients or pharmaceuticals for prevention of hypertension. (c) 2015 Elsevier Ltd. All rights reserved.

分类号： TS2`TS201.2

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