Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum

Lee, Dae Hyoung; Kim, Jae Ho; Park, Jeong Sik; Choi, Young Jun; Lee, Jong Soo

doi:10.1016/j.peptides.2004.01.015

Cited by 160 publications

(53 citation statements)

References 27 publications

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“…Chaurasia et al (2013a, b) have reported the maximum laccase activity at 40 °C. On the other hand, Tricarpelema giganteum (Hyoung et al 2004), Lentinula edodes (Sun et al 2011), Pleurotus eryngii (Wang and Ng 2006b), and Ganoderma lucidum (Wang and Ng 2006a) laccases demonstrated a higher optimal temperature of 70 °C. Farnet et al (2000) described a laccase from Marasmius quercophilus , a white-rot fungus, with temperature optimum at 80 °C.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Vantamuri

Kaliwal

2016

3 Biotech

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A novel laccase-producing white-rot fungus, Marasmius sp. BBKAV79 (Genbank Accession Number-KP455496, KP455497), was isolated and subjected to purification, characterization and dye decolorization study. The purified enzyme was obtained with a specific activity of 0.226 U mg -1 protein and a final yield of 13.5 %. The enzyme was found to be a monomeric protein with a molecular mass of *75 kDa as estimated by non-denaturing polyacrylamide gel electrophoresis (PAGE) and further confirmed with zymogram analysis. The optimal pH and temperature of the laccase was recorded to be 5.5 and 40°C, respectively. The metal ions Hg 2? and Ag ? were found to drastically inhibit the activity of laccase at the rate of 96.6 and 96.5 %, respectively. Nevertheless, Fe 3? was found to inhibit laccase activity at 40 %. Phenylmethanesulfonyl fluoride (PMSF) strongly inhibited the laccase activity, and additives viz, sodium dodecyl sulfate (SDS), hydrogen peroxide (H 2 O 2 ) and sodium chloride (NaCl) were known to follow the earlier pattern of enzyme inhibition. The values of kinetic parameters K m and V max for purified laccase were noted at 3.03 mM and 5 lmol min -1 , respectively, for guaiacol as substrate. The textile dyes were decolorized at a range of 72-76 % and 88-93 % when treated with Marasmius sp. BBKAV79 and purified laccase, respectively. Based on the outcome of the present investigation, it could be, therefore, inferred that laccase isolated from Marasmius sp. BBKAV79 effectively decolorizes the textile dyes; however, the metal ions Hg 2? , Ag ? and Fe 3? and agents like PMSF, SDS, H 2 O 2 and NaCl pose an effective inhibitory potential under specified physicochemical conditions.

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Vantamuri

Kaliwal

2016

3 Biotech

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“…For example, few peptides, which exerted antihypertensive activity, were detected in garlic (Allium sativum L) (Suetsuna, 1998), in various kind of mushrooms (Pholiota adiposa, Tricholoma giganteum) (Hyoung et al, 2004;Koo et al, 2006), in soypaste (Shin et al, 2001), and in different kinds of cheeses (gouda, manchego, and varieties of Spanish and Swiss cheeses) (Saito et al, 2000;Gómez-Ruiz et al, 2002;Gómez-Ruiz et al, 2006;Meyer et al, 2009). These peptides can simply be extracted with water or alcohols like ethanol or methanol.…”

Section: Release Of Antihypertensive Peptides From Foodstuffsmentioning

confidence: 99%

“…The pure peptide can be submitted to a simulated gastrointestinal digestion using different enzyme systems. A combination of trypsin-chymotrypsin (Rizzello et al, 2008), pepsin-pancreatin (Robert et al, 2004), pepsin-corolase PP (Quiros et al, 2005), pepsin-trypsin (Koo et al, 2006) or pepsin-trypsin-protease N (Hyoung et al, 2004) enzymes have been employed for this purpose. This procedure has been assayed with peptides isolated from sea cucumber (Zhao et al, 2009), rice (Kuba et al, 2009), oyster (Wang et al, 2008a), porcine hemoglobin , and wakame (Sato et al, 2002) hydrolysates.…”

Section: Identification and Characterization Of Bioactive Peptides Frmentioning

confidence: 99%

“…However, the most favorable are aromatic amino acid residues and proline . Competitive ACE inhibitor peptides have been found inter alia in porcine skeletal muscle troponin (Katayama et al, 2008), soybean glycinin (Gouda et al, 2006), Pholiota adiposa (Koo et al, 2006), oyster (Je et al, 2005a), mushroom Tricholoma giganteum (Hyoung et al, 2004), and porcine hemoglobin hydrolysates. Noncompetitive ACE inhibitor peptides have been found in oyster (Wang et al, 2008a), tuna dark muscle (Qian et al, 2007a), bullfrog muscle (Qian et al, 2007b), pork loin (Katayama et al, 2007), bovine lactoferrin (Lee et al, 2006a), and hen ovotransferrin hydrolysates (Lee et al, 2006b).…”

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confidence: 99%

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Isolation and Characterization of Peptides with Antihypertensive Activity in Foodstuffs

Puchalska

Marina

García

2014

Critical Reviews in Food Science and Nutrition

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Hypertension is one of the main causes of cardiovascular diseases. Synthetic drugs inhibiting ACE activity present high effectiveness in the treatment of hypertension but cause undesirable side effects. Unlike these synthetic drugs, antihypertensive peptides do not show any adverse effect. These peptides are naturally present in some foods and since hypertension is closely related to modern diet habits, the interest for this kind of foods is increasing. Different methods for the purification, isolation, and characterization of antihypertensive peptides in foods have been developed. Nevertheless, there is no revision work summarizing and comparing these strategies. In this review, in vivo and in vitro pathways to obtain antihypertensive peptides have been summarized. The ACE mechanism and the methodologies developed to assay the ACE inhibitory activity have also been described. Moreover, a comprehensive overview on the isolation, purification, and identification techniques focusing on the discovery of new antihypertensive peptides with high activity has been included. Finally, it is worthy to highlight that the quantitation of antihypertensive peptides in foods is a new trend since genotype and processing conditions could affect their presence. Analytical methodologies using mass spectrometry constitute an interesting option for this purpose.

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“…3.4.15.1) is a Zn-metallopeptidase that needs zinc and chloride for activation and plays a key physiological role in the control of blood pressure via the rennin-angiotensin system and kallikreinkinin system (Lee et al 2004). ACE acts as an exopeptidase that cleaves dipeptides from the C-terminus of various oligopeptides (Carl Curtiss et al 1978;Yang et al 1971), and it cleaves the C-terminal of histidyl-leucine of the inactive decapeptide angiotensin I to form the octapeptide angiotensin II, a potent vasoconstrictor, and inactivates catalytic function of bradykinin, a vasodilatory agent (Hollenberg 1979;Yang 1970).…”

Section: Introductionmentioning

confidence: 99%

Purification and Identification of a Novel Angiotensin I-Converting Enzyme Inhibitory Peptide from Sesame Meal

Liu

Cheng

Liu

et al. 2015

Int J Pept Res Ther

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An angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated and identified from sesame meal by successive chromatography. Sesame meal hydrolysates were obtained by treatment with alcalase, papain, neutrase and pepsin. The ACE inhibitory activities of each hydrolysate were investigated and the alcalase produced hydrolysate with the highest ACE inhibitory activity. The protein hydrolysate generated with alcalase was then separated by an ultrafiltration membrane with 10 kDa molecular weight cut-off membranes, Sephadex G-50 and semi preparative reversed-phase high-performance liquid chromatography (RP-HPLC). Biological functions of all fractions were assayed, and Y4, a fraction from semi preparative RP-HPLC, was found to display the highest ACE inhibitory activity. The molecular weight of Y4 was 873.3 Da and the amino acid sequence was Tyr-Ala-HisTyr-Ser-Tyr-Ala determined by TOF-MS/MS. The IC 50 value for ACE inhibitory activity of fraction Y4 was 0.6 mg/mL. These results suggested that the sesame meal hydrolysates may be a beneficial ingredient for nutraceuticals and pharmaceuticals against hypertension and its related diseases.

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Isolation and characterization of a novel angiotensin I-converting enzyme inhibitory peptide derived from the edible mushroom Tricholoma giganteum

Cited by 160 publications

References 27 publications

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Purification and characterization of laccase from Marasmius species BBKAV79 and effective decolorization of selected textile dyes

Isolation and Characterization of Peptides with Antihypertensive Activity in Foodstuffs

Purification and Identification of a Novel Angiotensin I-Converting Enzyme Inhibitory Peptide from Sesame Meal

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