Angiotensin I-converting enzyme inhibitory activities of Chinese fermented soypaste and estimation of the inhibitory substances

Angiotensin I-converting enzyme (ACE) inhibitory activities of aqueous extracts of Chinese commercial soypaste were investigated in this work. Six samples from northern China showed potent ACE inhibitory activities with IC₅₀ values less than 40.0 μg/mL. ACE inhibitors in the sample with the strongest activity were purified by ultrafiltration, solid-phase extraction and gradient RP-HPLC. According to spectroscopic methods, a compound (M328.1) was separated as C₁₅H₂₁NO₇. It was supposed to be a conjugate of phenylalanine and glucose generated by Maillard reaction during soypaste production, providing support on the contribution of Maillard reaction products to the ACE inhibitory activity of the sample. Results further indicated that the total ACE inhibition by the sample occurred from the combined function of various bioactive substances, suggesting that Chinese soypaste could be a good source of ACE inhibitors for exploring functional foods or ingredients with antihypertensive effect.     

葵花籽多肽的制备及其降压活性研究

试验以低温脱脂葵花籽粕为原料,进行脱脂和脱绿原酸处理后,用碱性蛋白酶制备葵花籽多肽。以水解度和ACE抑制率为评价指标,对底物浓度、加酶量、酶解温度、酶解时间和pH值进行单因素试验,在此基础上采用响应面试验优化碱性蛋白酶制备葵花籽多肽的最佳水解工艺。结果表明:底物浓度为15g/mL、加酶量为3 700U/g、酶解温度为56℃和pH值为8.2的条件下水解3h,ACE抑制率可达63.74%。     

枯草杆菌蛋白酶对大豆胰蛋白酶抑制剂的水解钝化研究

研究了枯草杆菌蛋白酶(Subtilisin)对大豆胰蛋白酶抑制剂(STI)酶解活性的影响。实验在50℃,pH7.5条件下反应1h,并以BAPNA为底物,采用改进的方法测定枯草杆菌蛋白酶对大豆胰蛋白酶抑制剂的水解钝化程度,用SDS-PAGE方法和分子排阻色谱法研究其蛋白酶钝化敏感性。结果证明,枯草杆菌蛋白酶可以水解大部分的抑制剂,并通过SDS-PAGE进一步证实了比色法得出的结论。而由分子排阻色谱图可以分析得出抑制剂经枯草杆菌蛋白酶酶解后,活性降低。分析认为,可能是由于抑制剂中二硫键被打断使得其结构发生改变,同时生成大量复杂的小分子多肽物质。因此,可以推断大豆胰蛋白酶抑制剂的稳定性与二硫键的存在有关。     

Tannin fraction from Ampelopsis grossedentata leaves tea (Tengcha) as an antioxidant and α‐glucosidase inhibitory nutraceutical

Leaf of Ampelopsis grossedentata is a new resource of functional foods with healthful properties. Antioxidant and α‐glucosidase inhibitory activities of water extract (made in the style of drinking), tannin fraction (TF) and dihydromyricetin (DMY) from A. grossedentata leaves were evaluated. The main component of TF was identified as gallotannins. DPPH and ABTS radical scavenging activities and reducing power of TF were superior to those of water extract, however, inferior to those of DMY. In no PBS wash protocol of cellular antioxidant activity assay, DMY and TF exhibited similarly, while in PBS wash protocol, the value of TF was higher than that of DMY. In addition, TF possessed the highest α‐glucosidase inhibitory activities (IC₅₀ = 1.94 μg mL^?1), followed by water extract (IC₅₀ = 23.10 μg mL^?1) and DMY (IC₅₀ = 72.21 μg mL^?1). The strong α‐glucosidase inhibitory activity of TF may attribute to the binding capacity to enzymes, as confirmed by fluorescence analysis.     

鸭梨多酚氧化酶的特性及抑制剂研究

以邻苯二酚为底物，采用分光光度法在420nm处测定鸭梨多酚氧化酶（PPO）的活性，研究了不同底物、温度、pH值和底物浓度对其活性的影响，并建立了酶促褐变反应动力学方程，探讨了柠檬酸、EDTA、亚硫酸氢钠和抗坏血酸四种抑制剂对鸭梨酶促褐变的抑制效果。结果表明，鸭梨多酚氧化酶的最适底物为邻苯二酚，最适温度为30℃，最适pH为6．6；酶促褐变反应动力学符合米氏方程所描述的单底物酶促反应动力学，以邻苯二酚为底物的动力学参数Km=0．333mol／L，Vmax=0．089U／min。相应的动力学方程为v=0．089[S]／（0．333＋[S]；四种物质对该酶均表现出不同的抑制作用，抑制效果为：抗坏血酸〉EDTA〉柠檬酸〉亚硫酸氢钠。     

我国蛋白来源的血管紧张素转换酶抑制肽研究现状

概述了我国不同蛋白来源的血管紧张素转换酶抑制肽(ACEIP)的研究现状,并分析了现有研究存在的问题和发展趋势,旨在促进蛋白资源的有效利用和我国ACEIP的研究开发。     

Glycosidase inhibitory phenolic compounds from the seed of Psoralea corylifolia

The seeds of Psoralea corylifolia were extracted into five different polar solvents: chloroform, 50% ethanol in water, ethanol, methanol and water. All extracts were evaluated for glycosidase inhibitory activity. The chloroform extract (CE) showed the lowest IC₅₀ values against α-glucosidase (82.9 μg/ml) and α-mannosidase (132 μg/ml). Chromatography of CE yielded nine phenolic compounds which were identified as isovabachalcone (1), 4′-O-methylbavachalcone (2), isobavachromene (3), corylifolin (4), bavachinin (5), psoralidin (6), neobavaisoflavone (7), corylifol A (8), and bakuchiol (9). All isolated compounds, apart from compound 5, possessed α-glucosidase inhibitory activities. Among them, compounds 6–8 exhibited potent inhibition with IC₅₀s of 13.7, 27.7 and 11.3 μM, respectively. Furthermore, compounds 2 and 6 showed α-mannosidase inhibitory activity. Mechanistic analysis of their inhibition modes against α-glucosidase showed that compounds (6 and 7) were noncompetitive, whereas compound 8 was mixed. Furthermore, the most active glycosidase inhibitors (2, 6–8) were proven to be present in the native seed in high quantities by an HPLC chromatogram.     

Novel α-glucosidase inhibitors from Macaranga tanarius leaves

One of the hyperglycaemic remedies is glucose absorption reduction by suppressing carbohydrate digestion due to utilisation of α-glucosidase inhibitors (AGIs). Determination of prospecting herbs done in vitro by using enzyme assay resulted in the finding of Macaranga tanarius, which showed a potent inhibitory activity. An EtOAc-soluble extract of M. tanarius leaves was chromatographed by a Diaion HP-20 column and the active fractions were further purified with high performance liquid chromatography (HPLC) to isolate active principles against α-glucosidase. Five ellagitannins were successfully isolated and identified. Structure determination revealed that these isolated compounds were mallotinic acid (IC₅₀ > 5.00 mM), corilagin (IC₅₀ = 2.63 mM), chebulagic acid (IC₅₀ = 1.00 mM), and two novel compounds named macatannins A (IC₅₀ = 0.80 mM) and B (IC₅₀ = 0.55 mM). AGIs play an important role for the treatment of diabetes, therefore this research results may suggest novel alternatives for diabetes treatment management.     

Alcalase蛋白酶降解大豆胰蛋白酶抑制剂的研究

研究了不同酶解条件下 (pH值、温度、时间、加酶量和添加巯基还原剂 ) ,碱性内切蛋白酶Alcalase对大豆蛋白和大豆胰蛋白酶抑制剂的降解作用。研究结果表明 ,Alcalase可同时降解大豆蛋白和胰蛋白酶抑制剂。该酶解反应的最适条件为 :pH 8 0、温度 6 0℃、最适加酶量 10 μL/g蛋白 (约 0 0 2 832AU/ g蛋白 ) ,添加Na2 SO3为ω(Na2 SO3) =0 3% ,水解时间 4h。在此条件下 ,残留胰蛋白酶抑制活性为对照的 2 0 % ,可溶性蛋白含量可达 2 7mg/mL ,游离氨基酸含量为 7 1mg/mL ,大豆蛋白的水解度为 8 9%。还讨论了Alcalase蛋白酶降解大豆蛋白生成小肽的最佳反应条件     

INHIBITION OF BEER-SPOILAGE LACTIC ACID BACTERIA BY NISIN

149 strains of bacteria, mostly brewery contaminants able to spoil wort or beer, and 12 brewing strains of yeast (8 ale and 4 lager strains) have been screened using a well-test assay for sensitivity to the food preservative, Nisin (E234), Nisin inhibited growth of 92% of the gram-positive strains, predominantly lactic acid bacteria of the genera Lactobacillus and Pediococcus. In contrast, all 32 gram-negative strains tested, except 3 Flavobacter strains, were Nisin-resistant; in addition none of the brewing yeasts showed Nisin-sensitivity. Therefore. Nisin has potential applications in preventing spoilage of worts or beers by lactic acid bacteria.