大豆蛋白经体外胃蛋白酶-胰蛋白酶消化产生的血管紧张素I转换酶抑制肽。

Angiotensin I converting enzyme inhibitory peptides from in vitro pepsin-pancreatin digestion of soy protein.

作者信息

Lo Wendy M Y, Li-Chan Eunice C Y

机构信息

The University of British Columbia, Faculty of Agricultural Sciences, Food Science Building, 6650 N.W. Marine Drive, Vancouver, British Columbia V6T 1Z4, Canada.

出版信息

J Agric Food Chem. 2005 May 4;53(9):3369-76. doi: 10.1021/jf048174d.

DOI:10.1021/jf048174d

PMID:15853374

Abstract

Angiotensin I converting enzyme (ACE) inhibitory activity was determined in the soy protein isolate (SPI) digest produced by in vitro pepsin-pancreatin sequential digestion. The inhibitory activity was highest within the first 20 min of pepsin digestion and decreased upon subsequent digestion with pancreatin. An IC(50) value of 0.28 +/- 0.04 mg/mL was determined after 180 min of digestion, while no ACE inhibitory activity was measured for the undigested SPI at 0.73 mg/mL. Chromatographic fractionation of the SPI digest resulted in IC(50) values of active fractions ranging from 0.13 +/- 0.03 to 0.93 +/- 0.08 mg/mL. Although many of the fractions showed ACE inhibition, peptides with lower molecular masses and higher hydrophobicities were most active. The findings show that many different peptides with ACE inhibitory activities were produced after in vitro pepsin-pancreatin digestion of SPI and lead to the speculation that physiological gastrointestinal digestion could also yield ACE inhibitory peptides from SPI.

摘要

通过体外胃蛋白酶 - 胰酶顺序消化产生的大豆分离蛋白（SPI）消化物中的血管紧张素I转换酶（ACE）抑制活性进行了测定。在胃蛋白酶消化的前20分钟内抑制活性最高，随后用胰酶消化时活性降低。消化180分钟后测定的IC（50）值为0.28±0.04 mg/mL，而对于浓度为0.73 mg/mL的未消化SPI未检测到ACE抑制活性。SPI消化物的色谱分离产生的活性级分的IC（50）值范围为0.13±0.03至0.93±0.08 mg/mL。虽然许多级分显示出ACE抑制作用，但分子量较低和疏水性较高的肽活性最高。研究结果表明，SPI经体外胃蛋白酶 - 胰酶消化后产生了许多具有ACE抑制活性的不同肽，这引发了一种推测，即生理条件下的胃肠道消化也可能从SPI中产生ACE抑制肽。