Studies on Biologically Active Peptides Produced by Phytoplankton

1. 生物活性肽的筛选收集了24种和菌株的藻类样品并进行了培养。研究了其水溶性和脂溶性组分中血管紧张素转换酶、木瓜蛋白酶、弹性酶、胰蛋白酶和凝乳胰蛋白酶的抑制活性。11种的水溶性组分和8种的脂溶性组分表现出抑制血管紧张素转换酶的活性。14种的水溶性组分和23种的脂溶性组分对木瓜蛋白酶活性有抑制作用。一种植物的水溶性组分和两种植物的脂溶性组分抑制弹性酶活性。5种的水溶性组分和11种的脂溶性组分对胰蛋白酶活性有抑制作用。其中5种的水溶性组分和8种的脂溶性组分对胰凝乳酶活性有抑制作用。血管紧张素转换酶抑制肽的分离和结构分析从杜氏绿藻和布朗杆菌中分离得到了血管紧张素转换酶抑制剂。根据水解产物的氨基酸分析结果，这些抑制剂被认为是多肽。在50马克杯/毫升时抑制血管紧张素转换酶。采用离子交换和反相色谱法从铜绿微囊藻中分离到一种血管紧张素转换酶抑制剂。通过氨基酸分析、FABMS和二维NMR鉴定其结构为1。该抑制剂包括一种新型氨基酸，2-氨基-3-羟基-8-甲基壬酸。7马克杯/毫升抑制血管紧张素转换酶。

1. Screening of biologically active peptidesAlgal samples of twenty four species and strains were collected and cultured. They were searched for angiotensin-converting enzyme, papain, elastase, trypsin and chymotrypsin inhibitory activities in their water-soluble and fat-soluble fractions. Water-soluble fractions of eleven species and fat-soluble fractions of eight species showed angiotensin-converting enzyme inhibitory activities. Water-soluble fractions of fourteen species and fat-soluble fractions of twenty three species inhibited papain activities. Water-soluble fraction of a species and fat-soluble fractions of two species inhibited elastase activities. Water-soluble fractions of five species and fat-soluble fractions of eleven species inhibited trypsin activities. Water-soluble fractions of five species and fat-soluble fractions of eight species inhibited chymotrypsin activities.2. Isolation and structural elucidation of angiotensin-converting enzyme inhibitory peptidesAngiotensin-converting enzyme inhibitors were isolated from water-soluble fractions of chlorophytes Dunaliella bardawil and Botryococcus braunii. These inhibitors were suggested to be peptides from the results of the hydrolysates amino acid analyses. They inhibited angiotensin-converting enzyme at 50 mug/ml.An angiotensin-converting enzyme inhibitor was isolated from the cyanophyte Microcystis aeruginosa by ion exchange and reverse phase chromatography. Its structure was determined as 1 by using amino acid analysis, FABMS and 2D NMR spectrum. The inhibitor includes a novel amino acid, 2-amino-3-hydroxy-8-methylnonanoic acid. It inhibited angiotensin-converting enzyme at 7 mug/ml.