|
| ||
|
|
||
ACE Inhibitory Activity (ace + inhibitory_activity)
Selected AbstractsEVALUATION OF RED CURRANTS (RIBES RUBRUM L.), BLACK CURRANTS (RIBES NIGRUM L.), RED AND GREEN GOOSEBERRIES (RIBES UVA-CRISPA) FOR POTENTIAL MANAGEMENT OF TYPE 2 DIABETES AND HYPERTENSION USING IN VITRO MODELSJOURNAL OF FOOD BIOCHEMISTRY, Issue 3 2010MARCIA DA SILVA PINTO ABSTRACT Red currants (Ribes rubrum L.), black currants (Ribes nigrum L.), red and green gooseberries (Ribes uva-crispa) were evaluated for the total phenolics, antioxidant capacity based on 2, 2-diphenyl-1-picrylhydrazyl radical scavenging assay and functionality such as in vitro inhibition of ,-amylase, ,-glucosidase and angiotensin I-converting enzyme (ACE) relevant for potential management of hyperglycemia and hypertension. The total phenolics content ranged from 3.2 (green gooseberries) to 13.5 (black currants) mg/g fruit fresh weight. No correlation was found between total phenolics and antioxidant activity. The major phenolic compounds were quercetin derivatives (black currants and green gooseberries) and chlorogenic acid (red currants and red gooseberries). Red currants had the highest ,-glucosidase, ,-amylase and ACE inhibitory activities. Therefore red currants could be good dietary sources with potential antidiabetes and antihypertension functionality to compliment overall dietary management of early stages of type 2 diabetes. [source] Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalaseANIMAL SCIENCE JOURNAL, Issue 1 2009Fu-Yuan CHENG ABSTRACT This study aims to identify peptides with angiotensin-I converting enzyme (ACE) inhibitory activity in hydrolysate from chicken leg bone protein hydrolyzed with alcalase for 4 h (A4H). The hydrolysate has demonstrated potent in vitro ACE inhibitory activity, and has been shown to attenuate the development of hypertension and cardiovascular hypertrophy in spontaneously hypertensive rats (SHR). A4H is competitive for ACE and was separated using high-performance liquid chromatography (HPLC) with a gel filtration column (Superdex Peptide HR 10/30). The results show that A4H is a mixed non-competitive inhibitor. Eighteen fractions were detected after separation of A4H, and most of them showed ACE inhibitory activity. Five fractions with strong ACE inhibitory activities (above 50%) were labeled from A to E. In addition, there were 10 peptides, consisting of 5,10 amino acid residues that were identified from fraction D that exhibited the strongest ACE inhibitory activity. Three of the identified peptides corresponded to peptides derived from collagen type I and chicken muscular protein. It is revealed that A4H has several peptides that possess ACE inhibitory activities. [source] Angiotensin I-converting enzyme inhibitory activity of Acetes chinensis peptic hydrolysate and its antihypertensive effect in spontaneously hypertensive ratsINTERNATIONAL JOURNAL OF FOOD SCIENCE & TECHNOLOGY, Issue 10 2009Chaohua Zhang Summary Peptic hydrolysate with angiotensin I-converting enzyme (ACE) inhibitory activity was prepared from Acetes chinensis. The 3 kDa ultrafiltration filtrates (UF-IV) of the desalted hydrolysate exerted a potent ACE inhibitory activity with IC50 being 0.67 mg mL,1. The fractions with molecular weight located between 611 and 240 Da achieved a total percentage of 63.6% in the UF-IV, with a mean peptide length of about 5.6,2.1. Gastrointestinal digestions were simulated on the hydrolysate and UF-IV and addressed their effect on the ACE inhibitory activity. The ACE inhibitory activity of the UF-IV could survive or be maintained in active form by simulated gastrointestinal digestion. Furthermore, the UF-IV exerted potent antihypertensive effect after oral administrations were given to spontaneously hypertensive rats (SHR) at a dose of 900 mg kg,1 body weight. In conclusion, the UF-IV could serve as useful antihypertensive peptides in the prevention and treatment of hypertension and other associated disorders. [source] The Potential Antioxidant Capacity and Angiotensin I-Converting Enzyme Inhibitory Activity of Monascus -Fermented Soybean Extracts: Evaluation of Monascus -Fermented Soybean Extracts as Multifunctional Food AdditivesJOURNAL OF FOOD SCIENCE, Issue 3 2007Y.-H. Pyo ABSTRACT:, The potential antioxidant capacity and angiotensin I-converting enzyme (ACE) inhibitory activity of Monascus -fermented soybean extracts (MFSE) were investigated. The average antioxidant capacities of 70% ethanol extracts from soybean after fermenting for 15 d at 30 °C were increased by a 5.2 to 7.4-fold (0.26 mM trolox equivalent/g dry weight, 91.7% 1,1-diphenyl-2-picrylhydrazyl [DPPH] radical scavenging effect at 3 mg/mL) when compared with those of the unfermented soybean extracts (P < 0.01). The potentially significant antioxidant properties of MFSE are associated with its content of bioactive mevinolins (r= 0.85) and isoflavone aglycones (r= 0.98), which were derived from the soybean during Monascus -fermentation. It was also found that the water extract having a molecular mass 1 to 3 kDa showed the highest ACE inhibitory activity (65.3%), which was remarkably greater (6.5 times) than the control. [source] Probiotic Strains as Starter Cultures Improve Angiotensin-converting Enzyme Inhibitory Activity in Soy YogurtJOURNAL OF FOOD SCIENCE, Issue 8 2005O.N. Donkor ABSTRACT Suitability of soy yogurt as a system for delivering probiotics and other bioactive compounds was assessed by fermenting soy milk using starter culture containing Lactobacillus delbrueckii ssp. bulgaricus Lb1466, Streptococcus thermophilus St1342, and probiotic organisms (Lactobacillus acidophilus LAFTI® L10, Bifidobacterium lactis LAFTI® B94, and Lactobacillus paracasei LAFTI® L26). Fermentations were terminated at different pH of 4.50, 4.55, and 4.60 and metabolic patterns of cultures (viability, proteolytic activity, organic acids production, angiotensin-converting enzyme (ACE) inhibitory activity) were investigated during 28 d of storage at 4 °C. The presence of probiotics enhanced the growth of L. delbrueckii ssp. bulgaricus Lb1466 and S. thermophilus St134 in soy yogurt in comparison to the control produced by sole yogurt culture. In general, different termination pH had no effect (P > 0.05) on the viability of probiotic organisms that maintained good viability in soy yogurt during cold storage. Higher levels of essential growth factors in the form of peptides and amino acids in soy yogurts may have promoted the growth of L. acidophilus LAFTI® L10, B. lactis LAFTI® B94, and L. paracasei LAFTI® L26. The use of probiotic strains as a part of starter culture in soy yogurt resulted in a substantial increase in in vitro ACE inhibitory activity compared with the control produced by yogurt culture only. This improvement of ACE inhibition in soy yogurt is partly due to higher proteolytic activity of probiotics. [source] The influence of fig proteases on the inhibition of angiotensin I-converting and GABA formation in meatANIMAL SCIENCE JOURNAL, Issue 6 2009Jinyue LI ABSTRACT The purposes of this research were to use fig protease for texture tenderizing, and to inhibit angiotensin I-converting enzyme (ACE) action and ,-aminobutyric acid (GABA) formation of meat. Liberated peptides by the enzymatic action of fig protease in processing meat and free amino acids were determined and ACE inhibitory activity was assayed. Meat treated with fig protease became tender as indicated by shear force value (SFV) which was half of those of non-fig treated meat during storage even at 5°C. Liberated peptides, free amino acids and GABA increased while extremely low levels of Glu were detected after storage. The optimal temperature of fig protease against meat was 80°C. However, the activity of fig protease decreased after pre-heating more than 40°C. High ACE inhibitory activity of a mixture of fig and meat was found around 80°C, and the value corresponded to the amount of liberated peptide. A lot of liberated peptides were found at 60,80°C and pasterization of meat product becomes convenient to produce peptides. Production of ACE inhibitory peptides and GABA can be expected as the healthy functional meat product such as antihypertensive activity and improve brain function. [source] Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalaseANIMAL SCIENCE JOURNAL, Issue 1 2009Fu-Yuan CHENG ABSTRACT This study aims to identify peptides with angiotensin-I converting enzyme (ACE) inhibitory activity in hydrolysate from chicken leg bone protein hydrolyzed with alcalase for 4 h (A4H). The hydrolysate has demonstrated potent in vitro ACE inhibitory activity, and has been shown to attenuate the development of hypertension and cardiovascular hypertrophy in spontaneously hypertensive rats (SHR). A4H is competitive for ACE and was separated using high-performance liquid chromatography (HPLC) with a gel filtration column (Superdex Peptide HR 10/30). The results show that A4H is a mixed non-competitive inhibitor. Eighteen fractions were detected after separation of A4H, and most of them showed ACE inhibitory activity. Five fractions with strong ACE inhibitory activities (above 50%) were labeled from A to E. In addition, there were 10 peptides, consisting of 5,10 amino acid residues that were identified from fraction D that exhibited the strongest ACE inhibitory activity. Three of the identified peptides corresponded to peptides derived from collagen type I and chicken muscular protein. It is revealed that A4H has several peptides that possess ACE inhibitory activities. [source] A rapid assay for angiotensin-converting enzyme activity using ultra-performance liquid chromatography,mass spectrometryBIOMEDICAL CHROMATOGRAPHY, Issue 3 2010Fang Geng Abstract Angiotensin-converting enzyme (ACE) plays an important role in the renin,angiotensin system and ACE activity is usually assayed in vitro by monitoring the transformation from a substrate to the product catalyzed by ACE. A rapid and sensitive analysis method or ACE activity by quantifying simultaneously the substrate hippuryl,histidyl,leucine and its product hippuric acid using an ultra-performance liquid chromatography coupled with electrospray ionization-mass spectrometry (UPLC-MS) was first developed and applied to assay the inhibitory activities against ACE of several natural phenolic compounds. The established UPLC-MS method showed obvious advantages over the conventional HPLC analysis in shortened running time (3.5,min), lower limit of detection (5,pg) and limit of quantification (18,pg), and high selectivity aided by MS detection in selected ion monitoring (SIM) mode. Among the six natural products screened, five compounds, caffeic acid, caffeoyl acetate, ferulic acid, chlorogenic acid and resveratrol indicated potent in vitro ACE inhibitory activity with IC50 values of 2.527 ± 0.032, 3.129 ± 0.016, 10.898 ± 0.430, 15.076 ± 1.211 and 6.359 ± 0.086,mm, respectively. A structure,activity relationship estimation suggested that the number and the situation of the hydroxyls on the benzene rings and the acrylic acid groups may play the most predominant role in their ACE inhibitory activity. Copyright © 2009 John Wiley & Sons, Ltd. [source] | ||||||||||