Angiotensin‐I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats

Katayama, Kazunori; Mori, Takeo; Kawahara, Satoshi; Miake, K; Kodama, Yoshiro; Sugiyama, Masaaki; Kawamura, Yukio; Nakayama, Toshihiro; Maruyama, Masugi; Muguruma, Michio

doi:10.1111/j.1750-3841.2007.00571.x

Cited by 60 publications

(39 citation statements)

References 23 publications

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“…Peptic hydrolysate of porcine crude myosin also had inhibitory activity with the 50% inhibitory value of 112 µg/mL (Katayama et al, 2003b). ACE inhibitory peptide had also derived from porcine skeletal muscle myosin and had antihypertensive activity in SHR (Katayama et al, 2007). The peptide was detected as an octapeptide, Val-Lys-Lys-Val-Leu-Gly-Asn-Pro, from 47 th to 54 th position of myosin light chain.…”

Section: Introductionmentioning

confidence: 97%

Purification of Angiotensin Converting Enzyme Inhibitory Peptide Derived From Kacang Goat Meat Protein Hydrolysate

Jamhari

Yusiati

Suryanto

et al. 2013

J. Indonesian Trop. Anim. Agric.

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ABSTRAKPenelitian ini bertujuan untuk mengidentifikasi peptida Angiotensin Converting Enzyme (ACE) inhibitor dari hidrolisat protein daging kambing Kacang. Daging kambing Kacang bagian loin dihidrolisis dengan enzim pepsin, trypsin dan chymotrypsin. Hidrolisat protein daging kemudian diuji konsentrasi protein dan aktivitas ACE inhibitor. Peptida ACE inhibitor dipurifikasi melalui serangkaian purifikasi dengan column SEP-PAK Plus C18 Cartridge dan RP-HPLC dengan menggunakan column Cosmosil 5PE-SM, 4,6 x 250 mm. Sekuen asam amino peptida ACE inhibitor kemudian diidentifikasi dengan menggunakan amino acids sequencer. Hasil purifikasi peptida menunjukkan bahwa sekuen asam amino peptida ACE inhibitor dari hidrolisat protein daging kambing Kacang adalah leu-thr-glu-ala-proleu-asn-pro-lys-ala-asn-arg-glu-lys. Peptida tersebut mempunyai berat molekul (BM) sebesar 1581 dan berada pada posisi residu ke-20 sampai ke-33 dari protein b-actin daging kambing (Capra hircus). Peptida tersebut mempunyai aktivitas ACE inhibitor (IC 50 ) sebesar 190 mg/mL atau 120 mM.Kata Kunci: Peptida ACE Inhibitor, hidrolisat protein daging, kambing Kacang ABSTRACTThe objective of this study was to identify the Angiotensin Converting Enzyme (ACE) inhibitory peptide derived from Kacang goat meat protein hydrolysate. Kacang goat meat loin section was hydrolyzed with pepsin, trypsin and chymotrypsin. Protein hydrolysate of Kacang goat meat was then tested the protein concentration and ACE inhibitory activity. ACE inhibitory peptide of the protein hydrolysate was purified through several steps of purification by column SEP-PAK Plus C18 Cartridge and RP-HPLC using a Cosmosil column 5PE-SM, 4.6 x 250 mm. The sequence of amino acid of ACE inhibitory peptide was identified by amino acid sequencer. The results showed that amino acids sequence of ACE inhibitory peptide derived from protein hydrolysate of Kacang goat meat was leu-thrglu-ala-pro-leu-asn-pro-lys-ala-arg-asn-glu-lys. It had a molecular weight (MW) of 1581 and occurred at the position of 20 th to 33 rd residues of b-actin of goat meat protein (Capra hircus). The ACE inhibitory activity (IC50) of the peptide was 190 mg/mL or 120 mM.

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Section: Introductionmentioning

confidence: 97%

Purification of Angiotensin Converting Enzyme Inhibitory Peptide Derived From Kacang Goat Meat Protein Hydrolysate

Jamhari

Yusiati

Suryanto

et al. 2013

J. Indonesian Trop. Anim. Agric.

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“…Tripeptide MNP (f79-81) exhibited enhanced ACE-inhibitory activity, compared to the parent myopentapeptide A, with IC 50 value of 66.6 μM (Arihara et al, 2001). Myosin as a source of bioactive peptides has also been used by Katayama et al (2007). By digestion of crude myosin light chain with pepsin, ACE-inhibitory octapeptide (VKKV-LGNP, f47-54, the IC 50 value of 28.5 μM) has been generated.…”

Section: Antihypertensive Propertiesmentioning

confidence: 99%

Meat and fermented meat products as a source of bioactive peptides

Stadnik

Kęska

2015

Acta Sci Pol Technol Aliment

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Bioactive peptides are short amino acid sequences, that upon release from the parent protein may play different physiological roles, including antioxidant, antihypertensive, antimicrobial, and other bioactivities. They have been identifi ed from a range of foods, including those of animal origin, e.g., milk and muscle sources (with pork, beef, or chicken and various species of fi sh and marine organism). Bioactive peptides are encrypted within the sequence of the parent protein molecule and latent until released and activated by enzymatic proteolysis, e.g. during gastrointestinal digestion or food processing. Bioactive peptides derived from food sources have the potential for incorporation into functional foods and nutraceuticals. The aim of this paper is to present an overview of the muscle-derived bioactive peptides, especially those of fermented meats and the potential benefi ts of these bioactive compounds to human health.

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“…Apart from drugs and snake venom, several dietary peptides, as well as other food components, such as calcium [63], γ-aminobutyric acid [39], exopolysaccharides from Lactobacillus [L.] casei [2], polyphenols in cocoa and tea [124] and nitrate from vegetables [135] or a diet rich in fruits, vegetables and low-fat dairy products [5], have been reported to be effective in lowering blood pressure. Using in vitro or in vivo experiments, ACEinhibiting activity has been found in a large number of products, such as fermented milk [27,42,49,52,76,79,80,109,138], hydrolysed food proteins [53], soya [54], zein [71,141], corn gluten meal [140], sorghum [45], potatoes [58,91], sesame [81], peanuts [98], algae [112], eggs [67,68,97], beef hydrolysates [40], porcine skeletal muscle [46,47], chicken breast muscle [104], chicken collagen hydrolysate [103], fish [20,60], sardine muscle [61], oysters [134], haemoglobin [70], royal jelly [62], coffee [101] and wine [93].…”

Section: Introductionmentioning

confidence: 99%

ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

Sieber

Bütikofer

Egger

et al. 2009

Dairy Sci. Technol.

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-During the ripening of cheese, a large number of peptides are formed from casein. Some of these peptides have been shown to exert an antihypertensive effect due to their angiotensin-I-converting enzyme (ACE)-inhibitory activity. Recently, several studies have investigated the ACE-inhibiting potential of cheese, and various ACE-inhibiting peptides have been isolated and identified from different cheese varieties. The present review focuses on the occurrence of two tripeptides, Val-Pro-Pro and Ile-Pro-Pro, in cheese. These tripeptides were first described in fermented-milk products and have been demonstrated to exert a blood pressure-lowering effect in humans with mild hypertension. The influence of cheesemaking and ripening on the release of ACE-inhibiting peptides is revealed. Finally, the antihypertensive potential of cheese with high ACE-inhibitory activity is discussed with regard to the bioavailability of the peptides involved.

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Angiotensin‐I Converting Enzyme Inhibitory Peptide Derived from Porcine Skeletal Muscle Myosin and Its Antihypertensive Activity in Spontaneously Hypertensive Rats

Cited by 60 publications

References 23 publications

Purification of Angiotensin Converting Enzyme Inhibitory Peptide Derived From Kacang Goat Meat Protein Hydrolysate

Purification of Angiotensin Converting Enzyme Inhibitory Peptide Derived From Kacang Goat Meat Protein Hydrolysate

Meat and fermented meat products as a source of bioactive peptides

ACE-inhibitory activity and ACE-inhibiting peptides in different cheese varieties

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