Purification of an ACE inhibitory peptide after hydrolysis of sunflower (Helianthus annuus L.) protein isolates

被引：180

作者：

Megías, C ^{[1
]}

Yust, MD ^{[1
]}

Pedroche, J ^{[1
]}

Lquari, H ^{[1
]}

Girón-Calle, J ^{[1
]}

Alaiz, M ^{[1
]}

Millán, F ^{[1
]}

Vioque, J ^{[1
]}

机构：

[1] Inst Grasa, Seville 41012, Spain

来源：

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY | 2004年 / 52卷 / 07期

关键词：

sunflower protein hydrolysate; ACE inhibitors; bioactive peptides; Helianthus annuus L;

D O I：

10.1021/jf034707r

中图分类号：

S [农业科学];

学科分类号：

09 ;

摘要：

Sunflower protein isolates and the proteases pepsin and pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-1 converting enzyme (ACE). Hydrolysates obtained after 3 h of incubation with pepsin and 3 h with pancreatin were studied. An ACE inhibitory peptide with the sequence Phe-Val-Asn-Pro-Gln-Ala-Gly-Ser was obtained by G-50 gel filtration chromatography and high-performance liquid chromatography C-18 reverse phase chromatography. This peptide corresponds to a fragment of helianthinin, the 11S globulin from sunflower seeds, which is the main storage protein in sunflower. These results show that sunflower seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with pepsin and pancreatin.

引用

页码：1928 / 1932

页数：5

共 45 条

[1] DETERMINATION OF THE DEGREE OF HYDROLYSIS OF FOOD PROTEIN HYDROLYSATES BY TRINITROBENZENESULFONIC ACID [J].