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1.
Isolation of peptides from a novel brewers spent grain protein isolate with potential to modulate glycaemic response
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Alan Connolly Martina B. O'Keeffe Alice B. Nongonierma Charles O. Piggott Richard J. FitzGerald 《International Journal of Food Science & Technology》2017,52(1):146-153
The in vitro dipeptidyl peptidase‐IV (DPP‐IV) inhibitory activity of a Brewers’ spent grain protein‐enriched isolate (BSG‐PI) Alcalase? hydrolysate (AlcH), which had previously been identified as a relatively potent angiotensin‐converting enzyme (ACE) inhibitor, was determined. The half maximal DPP‐IV inhibitory concentration (IC50) value of AlcH following 240‐min digestion was 3.57 ± 0.19 mg mL?1. Ultrafiltration fractionation did not significantly increase the DPP‐IV inhibitory activity of the AlcH fractions. Subjection of AlcH to simulated gastrointestinal digestion (SGID), which yielded SAlcH, resulted in a significant increase in DPP‐IV inhibitory activity (P < 0.05), particularly after the intestinal phase of digestion. Following semi‐preparative reverse phase high performance liquid chromatography (RP‐HPLC) fractionation of SAlcH, fraction 28 was identified as having highest mean DPP‐IV inhibitory activity. Two novel DPP‐IV inhibitory peptides, ILDL and ILLPGAQDGL, with IC50 values of 1121.1 and 145.5 μm , respectively, were identified within fraction 28 of SAlcH following ultra‐performance liquid chromatography (UPLC)‐tandem mass spectrometry (MS/MS). BSG protein‐derived peptides were confirmed as having dual ACE and DPP‐IV inhibitory activities. 相似文献
2.
Identification of angiotensin converting enzyme inhibitory and antioxidant peptides in a whey protein concentrate hydrolysate produced at semi‐pilot scale
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Martina B. O'Keeffe Celia Conesa Richard J. FitzGerald 《International Journal of Food Science & Technology》2017,52(8):1751-1759
Antioxidant and angiotensin converting enzyme (ACE) inhibitory peptides were identified in a 5 kDa ultrafiltration permeate of a whey protein hydrolysate generated at semi‐pilot scale. Further laboratory scale ultrafiltration of this 5 kDa permeate resulted in a 0.65 kDa permeate with antioxidant, (1.11 ± 0.074 μmol TE per mg dry weight, oxygen radical absorbance capacity, ORAC) and ACE inhibitory (ACE IC50 0.215 ± 0.043 mg mL?1) activities. Semi‐preparative (SP) reverse phase high‐performance liquid chromatography (RP‐HPLC) of the 0.65 kDa permeate resulted in a fraction (SP_F3) with a 4.4‐fold increase in ORAC activity (4.83 ± 0.45 μmol TE mg dry weight) and a 1.3‐fold increase in ACE inhibitory activity (84.35 ± 1.36% inhibition when assayed at 0.28 mg mL?1). Peptides within SP_F3 were identified using UPLC‐ESI‐MS/MS. Met‐Pro‐Ile had the highest ORAC activity (205.75 ± 12.08 μmol TE per mmol peptide) while Met‐Ala‐Ala and Val‐Ala‐Gly‐Thr had the highest ACE inhibitory activities (IC50:515.50 ± 1.11 and 610.30 ± 2.41 μm , respectively). 相似文献
3.
Ribbonfish (Trichiurus haumela) backbone is normally discarded as an industrial waste from fish processing. A method of developing angiotensin I‐converting enzyme inhibitory (ACEI) peptides from ribbonfish backbone was previously optimized. The purposes of the study were to characterize the active peptides in the hydrolysate and to evaluate its in vivo activity. Ribbonfish backbone protein hydrolysate prepared by acid protease was fractionated into 4 fractions (I, MW < 1 kDa; II, MW = 1 to 5 kDa; III, MW = 5 to 10 kDa; and IV, MW > 10 kDa) through ultrafiltration membranes. Fraction I, showing the highest ACEI activity, was further purified using consecutive chromatographic techniques including gel filtration and reversed phase high‐performance liquid chromatography. The purified ACE inhibitory peptide was determined to have a molecular weight of 317.25 Da, with a sequence of Leu‐Trp and an IC50 value of 5.6 μM. Systolic blood pressure of spontaneously hypertensive rats was significantly decreased from 181 ± 2.0 to 161.3 ± 2.3 mm Hg after 4 h of oral administration of Leu‐Trp at a dose of 10 mg/kg of body weight. These results indicated that ribbonfish backbone protein could be used for development of antihypertensive agent. 相似文献
4.
Junfeng Fan Xiaozhong Hu Szesze Tan Yanyan Zhang Eizo Tatsumi Lite Li 《Journal of the science of food and agriculture》2009,89(4):603-608
BACKGROUND: Douchi, a traditional fermented soybean food, has recently attracted a great deal of attention owing to its superior physiological activity. In the present study the angiotensin I‐converting enzyme (ACE)‐inhibitory activity of typical douchi procured from various regions of China was analysed. An ACE‐inhibitory peptide derived from the most potent douchi was also isolated and characterised. The pattern of ACE inhibition and resistance to hydrolysis by gastrointestinal proteases of this peptide are described. RESULTS: ACE‐inhibitory activities were detected in all douchi samples, with IC50 values ranging from 0.204 to 2.011 mg mL?1. Among the douchi samples, a Mucor‐type douchi exhibited the most potent ACE‐inhibitory activity (IC50 = 0.204 mg mL?1). A novel ACE‐inhibitory peptide was then isolated from this Mucor‐type douchi using ultrafiltration followed by Sephadex G‐25 column chromatography and reverse phase high‐performance liquid chromatography. The amino acid sequence of the purified peptide was identified by Edman degradation as His‐Leu‐Pro (IC50 = 2.37 µmol L?1). The peptide is a competitive inhibitor and maintained its inhibitory activity even after incubation with some gastrointestinal proteases. CONCLUSION: The present study shows that peptides derived from soybean fermentation during douchi processing could be the main contributor to the ACE‐inhibitory activity observed. Copyright © 2009 Society of Chemical Industry 相似文献
5.
A tryptic gliadin hydrolysate was fractionated into peptide fractions, which were assigned to either the central domain (CD) or terminal domains (TD) of gliadins. The domains were expected to contain amino acid (AA) sequences which, when released from the parent protein, inhibit the angiotensin I-converting enzyme (ACE), which plays a key role in regulating blood pressure. A proline (Pro) poor TD related fraction, containing the smallest peptides, showed the highest ACE inhibitory activity (IC50 = 0.33 mg/ml). Additional peptidases were selected based on their in silico predicted ability to release ACE inhibitory peptides. Further hydrolysis of the tryptic hydrolysate fractions with thermolysin, Clarex, Alcalase and Esperase increased ACE inhibitory activities. Immobilised Ni2+-ion affinity chromatography (IMAC) purification of a TD related peptide fraction obtained by sequential hydrolysis with trypsin and thermolysin yielded a fraction with an IC50 value of 0.02 mg/ml. This IMAC fraction was enriched in histidine and hydrophobic AA (Pro, Val, Ile, Leu and Phe). 相似文献
6.
Inhibition properties of dipeptides from salmon muscle hydrolysate on angiotensin I-converting enzyme 总被引:1,自引:0,他引:1
Seigo Ono Masashi Hosokawa Kazuo Miyashita & Koretaro Takahashi 《International Journal of Food Science & Technology》2006,41(4):383-386
We isolated Phe–Leu as an angiotensin I‐converting enzyme (ACE) inhibitor from hydrolysate of chum salmon muscle. The IC50 value of this peptide was 13.6 μm , and it showed non‐competitive inhibition. The reverse sequence dipeptide Leu–Phe also showed ACE inhibitory activity. However, Leu–Phe is much less inhibitory than Phe–Leu with an IC50 value of 383.2 μm . In addition, the inhibition mode was competitive. To investigate the relationship between dipeptide sequence and ACE inhibition properties, we further measured ACE inhibitory activity and inhibition mechanism using six Trp‐containing dipeptides, which had been identified from the same salmon muscle hydrolysate as ACE inhibitory peptides in a previous study. Peptides with Trp as the C‐terminal residue, Ala–Trp, Val–Trp, Met–Trp, Ile–Trp, Leu–Trp showed non‐competitive inhibition. On the other hand, reversed sequence peptides with Trp at the N‐terminal were competitive inhibitors, except Trp–Leu. These results indicate that the sequence of ACE inhibitory dipeptides can affect both inhibitory potency and the inhibition mechanisms. 相似文献
7.
IDENTIFICATION OF ANGIOTENSIN I-CONVERTING ENZYME INHIBITORY PEPTIDES DERIVED FROM THE PEPTIC DIGEST OF SOYBEAN PROTEIN 总被引:1,自引:0,他引:1
JIUN-RONG CHEN TAKASHI OKADA KOJI MURAMOTO KUNIO SUETSUNA SUH-CHING YANG 《Journal of Food Biochemistry》2002,26(6):543-554
Peptidic fractions which inhibit angiotensin I‐converting enzyme (ACE) were separated from peptic digests of soybean by ion exchange chromatography and gel filtration. Further separation of the peptidic fractions by ODS HPLC afforded active peptides, the amino add sequences of which were identified by Edman's procedure as: Ile‐Ata (inhibitory against ACE with an IC50of 153 μM), Tyr‐Leu‐Ala‐Gly‐Asn‐Gln (14 μM), Phe‐Phe‐Leu (37 μM), Ile‐Tyr‐Leu‐Leu (42 μM), and Val‐Met‐Asp‐Lys‐Pro‐Gln‐Gly (39 μM). The antihypertensive activity of the soybean peptides was also investigated. Peptide fractions (2.0 g/kg body weight, oral administration) markedly towered the blood pressure of spontaneously hypertensive rats (SHRs). 相似文献
8.
Angiotensin I‐converting enzyme inhibitory and Ca‐binding activities of peptides prepared from tuna cooking juice and spleen proteases
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Jirawadee Kasiwut Wirote Youravong Pittaya Adulyatham Nualpun Sirinupong 《International Journal of Food Science & Technology》2015,50(2):389-395
Tuna cooking juice is a by‐product from the tuna canning industry. In this study, tuna cooking juice was hydrolysed by proteases extracted from the spleen. Tuna cooking juice showed the highest ACE inhibitory and Ca‐binding activities after hydrolysis for 270 and 180 min, respectively. The hydrolysate was further fractionated by ultrafiltration. The permeate exhibited highest ACE inhibitory and Ca‐binding activities when passed through 1 and 5 kDa cut‐off membranes, respectively. Gel filtration chromatography was used to determine the MW of bioactive peptides that exhibited highest ACE inhibitory and Ca‐binding activities. Those peptides that exhibited highest ACE inhibitory and Ca‐binding activities were the MW range of 238–829 Da and 1355–1880 Da, respectively. These results suggest that the tuna cooking juice and the spleen protease extract are a potential source of bioactive peptides that can be utilised as bioactive ingredients in functional food and nutraceuticals. 相似文献
9.
Angiotensin I‐converting enzyme (ACE) inhibitory peptide was isolated from wheat gliadin hydrolysate prepared with acid protease. Consecutive purification methods were used for peptide isolation including ion‐exchange chromatography, size‐exclusion chromatography, and reverse‐phase high‐performance liquid chromatography. The amino acid sequence of this peptide was identified as Ile‐Ala‐Pro, and the ACE inhibitory activity (IC50 value) was 2.7 μM . The hypotensive activity of Ile‐Ala‐Pro on spontaneously hypertensive rats was investigated. This peptide inhibited the hypertensive activity of angiotensin I with intravenous injection, and decreased the blood pressure significantly with intraperitoneal administration. 相似文献
10.
Justo Pedroche María M Yust Julio Girn‐Calle Manuel Alaiz Francisco Milln Javier Vioque 《Journal of the science of food and agriculture》2002,82(9):960-965
Chickpea protein isolates and the protease alcalase were used for the production of protein hydrolysates that inhibit angiotensin I‐converting enzyme (ACE). The highest degree of inhibition was found in a hydrolysate obtained by 30 min of treatment with alcalase. This hydrolysate was used as starting material for the purification of ACE‐inhibitory peptides. After Biogel P2 gel filtration chromatography and HPLC C18 reverse phase chromatography, four peptides with ACE‐inhibitory activity were purified. Two of them were competitive inhibitors of ACE, while the other two were uncompetitive inhibitors. These results show that chickpea proteins are a good source of ACE‐inhibitory peptides when hydrolysed with the protease alcalase. © 2002 Society of Chemical Industry 相似文献
11.
Sunantha Ketnawa Shyam Suwal Jen-Yi Huang Andrea M. Liceaga 《International Journal of Food Science & Technology》2019,54(4):1062-1073
Microwave pretreatment and hydrolysis were applied to rainbow trout (Oncorhynchus mykiss) by-products to produce bioactive peptides with dual in vitro angiotensin-I converting enzyme (ACE) and dipeptidyl-peptidase IV (DPP-IV) inhibitory activities. Peptides were fractionated using the single step electrodialysis with ultrafiltration membrane (EDUF). Concentration of cationic peptides (CP) increased in the recovery solution, reaching 125 μg mL−1 after a 4-h treatment with migration rate of 15.68 ± 2.98 g m−2 h. CP fractions displayed ACE and DPP-IV I inhibitory properties, with IC50 values of 0.0036 mg mL−1 and 1.23 mg mL−1 respectively. The bioactivity was attributed to the low molecular weight peptides (300–500 Da) recovered. CP exhibited non-competitive inhibition patterns for ACE and DPP-IV, which were dose dependent. These results showed that bioactive peptides can successfully be separated from complex hydrolysate mixtures by EDUF. The fractionated peptides can serve as potential functional food ingredients or nutraceuticals for the management of hypertension and diabetes. 相似文献
12.
Masomeh Ghassem Keizo Arihara Abdul S. Babji 《International Journal of Food Science & Technology》2012,47(11):2444-2451
The angiotensin I‐converting enzyme (ACE)‐inhibitory activities of catfish (Clarias batrachus) muscle protein hydrolysates were investigated. Thermolytic digests of C. batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration, gel filtration and reversed‐phase high‐performance liquid chromatography (RP‐HPLC). The amino acid sequences of hydrolysates with the highest ACE‐inhibitory activities were determined using electrospray quadrupole time‐of‐flight tandem mass spectrometry (ESI‐TOFQ MS/MS). The sequences of GPPP (IC50 = 0.86 μm ) and IEKPP (IC50 = 1.2 μm ) corresponding to the fragments 986–989 and 441–445 of myosin‐I heavy chain were identified for the sarcoplasmic and myofibrillar protein hydrolysates, respectively. Peptide GPPP exhibited a mixed‐type inhibition whereas peptide IEKPP could only bind to the active sites of ACE. The results demonstrate that hydrolysates of C. batrachus muscle proteins obtained by thermolysin may contain bioactive peptides. 相似文献
13.
Protein hydrolysates are of a significant interest, due to their potential application as a source of bioactive peptides in
nutraceutical and pharmaceutical domains. The present study was focused on bovine hemoglobin hydrolysate obtained with pig
pepsin in the presence of 30% ethanol. This hydrolysate was fractioned by reversed-phase high-performance liquid chromatography
(RP-HPLC) into 12 major fractions (F1–F12). All fractions were analyzed by ESI/MS and ESI/MS/MS, in order to characterize and identify the peptides in these fractions.
This hydrolysis permitted to generate a new serial of bioactive peptides with both antimicrobial and ACE inhibitory activities.
Identified peptides were TKAVEHLDDLPGALSELSDLHAHKLRVDPVNFKLLSHSLL, LDDLPGALSELSDLHAHKLRVDPVNFKLLSHSL, KLLSHSL, and LLSHSL
corresponding respectively to the 67-106, 73-105, 99-105, and 100-105 fragments of the α chain of bovine hemoglobin. They
were the first found from bovine hemoglobin. These purified peptides have an antibacterial activity against four bacteria
strains: Kocuria luteus A270, Listeria innocua, Escherichia coli, and Staphylococcus aureus with a MIC between 187.1 and 35.2 μM. On the other hand, these peptides displayed at the same time ACE inhibitory activity
with an IC50 range from 42.55 to 1,095 μM. 相似文献
14.
Angiotensin I‐converting enzyme inhibitory peptides FQPSF and LKYPI identified in Bacillus subtilis A26 hydrolysate of thornback ray muscle
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Imen Lassoued Leticia Mora Ahmed Barkia M‐Concepción Aristoy Moncef Nasri Fidel Toldrá 《International Journal of Food Science & Technology》2016,51(7):1604-1609
Angiotensin I‐converting enzyme (ACE) inhibitory peptides have been searched in thornback ray (Raja clavata) muscle hydrolysed with Bacillus subtilis A26 proteases until a hydrolysis degree of 18.35%. The hydrolysate showed an IC50 of 0.83 mg mL?1. To identify peptides responsible for this activity, the extract was eluted through size‐exclusion chromatography and fractions collected. The highest ACE inhibitory activity was found for fractions F2 and F3 which had IC50 of 0.42 and 0.51 mg mL?1, respectively. These fractions were analysed by nano‐liquid chromatography coupled to tandem mass spectrometry (nLC‐MS/MS). A total of 131 and 108 peptide sequences mainly derived from actin, myosin heavy chain and procollagen alpha 1 chain proteins were identified in fractions F2 and F3, respectively. FQPSF and LKYPI showed the best results with an IC50 of 12.56 and 27.07 μM, respectively. These results prove the potential of thornback ray muscle hydrolysate as a source of ACE inhibitory peptides. 相似文献
15.
Wenhong Cao Chaohua Zhang Pengzhi Hong Hongwu Ji Jiming Hao 《International Journal of Food Science & Technology》2010,45(5):959-965
Acetes chinensis is a marine shrimp found in the coastal waters of China. The shrimp was hydrolysed by pepsin to prepare hydrolysates with angiotensin I‐converting enzyme (ACE) inhibitory activity. The hydrolysate with the highest ACE inhibitory activity resulted from a 3–5 h incubation at 45 °C and pH 2.5 with pepsin. Gel filtration and RP‐HPLC were used to separate ACE inhibitory peptides from the hydrolysate. The gel filtration fraction of the hydrolysate with a molecular weight range from 1320 Da to 311 Da exerted the highest ACE inhibition activity. This fraction was separated by RP‐HPLC into fifteen fractions, of which fraction F9 showed 92.7% of the ACE inhibition activity. Its peptide sequence was determined to be Leu–His–Pro. It showed a potent antihypertensive activity in spontaneously hypertensive rats. The results suggested that this peptide may be a potent ACE inhibitor which might be developed into a healthy food to lower blood pressure. 相似文献
16.
《Journal of dairy science》2022,105(3):1913-1928
An improved bioassay-guided fractionation was performed to effectively screen angiotensin-I converting enzyme inhibitory (ACEI) peptides from milk protein hydrolysate. The aqueous normal phase liquid chromatography, namely hydrophilic interaction liquid chromatography (HILIC), was used as a format of solid-phase extraction (SPE) short column for the first fractionation, then the HILIC-SPE fraction with the best ACEI activity (IC50 = 61.75 ± 5.74 µg/mL; IC50 = half-maximal inhibitory concentration) was obtained when eluted by 95% acetonitrile + 0.1% formic acid (fraction F1). The best HILIC-SPE fraction was further fractionated using reversed-phase (RP)-SPE short column. The best RP-SPE fraction was obtained when eluted by 20% acetonitrile + 0.1% formic acid (fraction P3) with an ACEI activity of IC50 36.22 ± 1.18 µg/mL. After the 2-step fractionation, the IC50 value of fraction P3 significantly decreased by 8.92-fold when compared with the crude hydrolysate. Several peptides were identified from fraction P3 using liquid chromatography-tandem mass spectrometry. The in silico analysis of these identified sequences based on the BIOPEP database predicted that HLPLPLL (HL-7) was the most active peptide against angiotensin-converting enzyme (ACE). The HL-7 derived from β-casein showed a potent ACEI activity (IC50 value is 16.87 ± 0.3 µM). The contents of HL-7 in the gastrointestinal protease hydrolysate and RP-SPE fraction originated from 1 mg of milk proteins were quantified using a multiple reaction monitoring mode upon liquid chromatography-tandem mass spectrometry analysis to give 19.86 ± 1.14 pg and 14,545.8 ± 572.9 pg, respectively. Besides, the kinetic study indicated that HL-7 was a competitive inhibitor and the result was rationalized using the docking simulation. The study demonstrated an efficient screening of ACEI peptides from commercially available milk powders using a simple SPE process instead of a sophisticated instrument such as HPLC. Moreover, the potent ACEI peptide HL-7 uncovered by this method could be a natural ACE inhibitor. 相似文献
17.
Optimization and Scale‐Up Preparation of Egg White Hydrolysate with Angiotensin I Converting Enzyme Inhibitory Activity
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Angiotensin I converting enzyme (ACE) plays an important role in regulation of blood pressure as it converts angiotensin I into angiotensin II (a potent vasoconstrictor). Food protein‐derived ACE inhibitory peptides have been considered as a safer alternative to antihypertensive drugs. In our previous study, three ACE inhibitory peptides were characterized from egg white ovotransferrin and their antihypertensive activity has been validated in spontaneously hypertensive rats. However, it is too costly to prepare these peptides from purified egg white ovotransferrin. The aims of the study were to determine the feasibility of preparing these peptides using egg white and then to optimize the conditions of preparing egg white hydrolysate. Taguchi's method was used to design experiments for optimization, which was established as follows: substrate %, pH of thermoase, time of thermoase digestion, ratio of pepsin to substrate, pH of pepsin, temperature of pepsin, and time of pepsin digestion were 7.5%, pH 8, 90 min, 1%, pH 2.5, 55 °C, and 180 min, respectively. The ACE inhibitory activity (IC50 value) and peptide yield obtained under optimal condition were 30 ± 2 μg/mL and 77.5% ± 0.3%, respectively, which were comparable to the predicted values. Hydrolysate prepared at 150 L reactor showed comparable activity but low peptide yield. Results of this study demonstrated the feasibility of using egg white protein as the starting material to prepare a functional ingredient with potent ACE inhibitory activity. 相似文献
18.
Seok-Chun Ko Min Cheol Kang Jung-Kwon Lee Hee-Guk Byun Se-Kwon Kim Seung-Cheol Lee Byong-Tae Jeon Pyo-Jam Park Won-Kyo Jung You-Jin Jeon 《European Food Research and Technology》2011,233(6):915-922
Angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated from Styela plicata. The S. plicata was hydrolyzed with various proteases including Protamex, Kojizyme, Neutrase, Flavourzyme, Alcalase, trypsin, α-chymotrypsin,
pepsin, and papain. The hydrolysate prepared with Protamex had the highest ACE inhibitory activity compared to the other hydrolysates.
We attempted to isolate ACE inhibitory peptides from hydrolysate prepared with Protamex using ultra-filtration, gel filtration
on a Sephadex G-25 column and reversed-phase high-performance liquid chromatography (RP-HPLC) on an ODS column. IC50 value of the purified ACE inhibitory peptide was 24.7 μM, and Lineweaver–Burk plots suggest that the purified peptide from
S. plicata acts as mixed-type inhibitor against ACE. Amino acid sequence of the purified peptide was identified as Met-Leu-Leu-Cys-Ser,
with a molecular weight 566.4 Da. The results of this study suggest that peptides derived from S. plicata may be beneficial as anti-hypertension compounds in functional foods resource. 相似文献
19.
Vanessa Vermeirssen John Van Camp Willy Verstraete 《Journal of the science of food and agriculture》2005,85(3):399-405
In vitro gastrointestinal digestion of pea and whey protein produced high angiotensin I converting enzyme (ACE) inhibitory activity with IC50 values of 0.070 and 0.041 mg protein ml?1 respectively. Ultrafiltration/centrifugation using a membrane with a molecular weight cut‐off of 3000 Da decreased the IC50 value to 0.055 mg protein ml?1 for pea permeate and 0.014 mg protein ml?1 for whey permeate. Further fractionation by reverse phase HPLC gave IC50 values as low as 0.016 mg protein ml?1 for pea and 0.003 mg protein ml?1 for whey. Consequently, these purification steps enriched the ACE inhibitory activity of the pea digest more than four times and that of the whey digest more than 13 times. HPLC profiles after digestion and ultrafiltration indicate that high ACE inhibitory activity is due to short and more hydrophobic peptides. The results also suggest that potent ACE inhibitory peptides were present alongside low active peptides in whey hydrolysate, while all peptides had more or less the same ACE inhibitory activity in pea hydrolysate. In addition, the hydrolysates and enriched fractions will resist in vivo gastrointestinal digestion after oral administration. Hence these ACE inhibitory peptides, as part of functional foods, can play significant roles in the prevention and treatment of hypertension. Copyright © 2004 Society of Chemical Industry 相似文献
20.
Shuang quan Harutoshi Tsuda Taku Miyamoto 《Journal of the science of food and agriculture》2008,88(15):2688-2692
BACKGROUND: Angiotensin I‐converting enzyme (ACE) is a dipeptidyl carboxypeptidase associated with the regulation of blood pressure. ACE inhibition results in a lowering of blood pressure. Lactic acid bacteria are known to produce ACE inhibitors during fermentation. Fermented camel milk is the main traditionally fermented dairy food for desert nomads. The beneficial effects of fermented camel milk, which include the prevention of such diseases and conditions as gastroenteritis, tuberculosis and hypertension, have been demonstrated experimentally. RESULTS: ACE inhibitory activity was observed in fermented milk containing Lactobacillus helveticus 130B4, a strain isolated from traditionally fermented camel milk. The peptide that inhibited ACE was purified from the fermented milk by reverse‐phase high‐performance liquid chromatography. The amino acid sequence of the peptide was identified as Ala‐Ile‐Pro‐Pro‐Lys‐Lys‐Asn‐Gln‐Asp (IC50 = 19.9 µmol L?1). The same Ala‐Ile‐Pro‐Pro‐Lys‐Lys‐Asn‐Gln‐Asp sequence was found in κ‐casein (κ‐CN) f107–115 from milk. The inhibitory activity of this nonapeptide (κ‐CN f107–115) was almost preserved even after successive digestion with pepsin, trypsin and chymotrypsin. Furthermore, the inhibitory activity of the purified peptide was completely preserved after heat treatment at 100 °C for 20 min. CONCLUSION: The fermented milk prepared with Lactobacillus helveticus 130B4 contained an ACE inhibitory peptide, κ‐CN 107–115. This fermented milk was expected to have anti‐hypertensive effect after ingestion because the peptide was stable to digestive protease and heat treatment in vitro. Copyright © 2008 Society of Chemical Industry 相似文献