Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of hydrolysates generated from byproducts of freshwater clam

Sun, Yi; Hayakawa, Shigeru; Ogawa, Masahiro; Naknukool, Supaporn; Guan, Yupin; Matsumoto, Yoshiyuki

doi:10.1007/s10068-011-0043-4

Cited by 12 publications

(6 citation statements)

References 23 publications

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“…Similarly results were also reported that antioxidant agent changed to the pro-oxidant activity at high protein hydrolysate concentration, such as resveratrol [22], lipolic acid and dihydrolipic acid [23]. Beside it is also reported that antioxidant of protein hydrolysates had molecular weight range from551 Da up to 3kDa [7][8][9][10]. Therefore the protein of nyamplung has to be hydrolysed to breakdown the peptide binding to short chain peptide to obtain the antioxidant activity.…”

Section: Antioxidant Activity Of Nyamplunghydrolysatementioning

confidence: 84%

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Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

Yanti¹,

Hastuti²,

Sulistyo³

et al. 2016

AIP Conference Proceedings

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Abstract. The seedcake of nyamplung seeds still contains high protein. Recent studies show that protein hydrolysate has many useful effects, such as an antioxidant. The protein was isolated by the isoelectric precipitation method, further on hydrolysed into short chain peptides. The chemical composition of seedcake and the protein content of extract were analysed. The hydrolysis of the extract was carried out in a various condition such as substrate concentration, pH, and temperature for a different length of hydrolysis and the degree of hydrolysis was determine by TNBS method. The protein isolation process performed on the defatted seedcake produced 52.84 ± 0.07% of protein extract with a brownish colour. The degree of hydrolysis (DH) was increased by increasing the length of hydrolysis and showed the optimum DH with 6.15mg/mL substrate concentration. The increase of temperature also increased the DH, however at 70°C with 240 min time reaction, the DH tended to decrease. The pH of reaction between papain showed the similar DH among various pH of the reaction, with pH 7 showed the stable increasing DH till 240 min of reaction. The antioxidant activity showed an increase to 90% of inhibition by the addition of the hydrolysate to the system until 1300 ppm. However, the addition of more than 1300 ppm showed a reduction activity

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Section: Antioxidant Activity Of Nyamplunghydrolysatementioning

confidence: 84%

“…The amino acid sequence of the peptide might play an important role in its activity. The molecular weight of protein hydrolysates that is ranging from 551 Da up to 3 k Da had the antioxidant activity [7][8][9][10].…”

Section: Introductionmentioning

confidence: 99%

Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

Yanti¹,

Hastuti²,

Sulistyo³

et al. 2016

AIP Conference Proceedings

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“…Lineweaver-Burk plots were applied to measure Michaelis-Menten equation and inhibition kinetics (Barbana & Boye 2011). Inhibition constants (K i ) were determined from the Lineweaver-Burk plots, and calculated by the equation (Sun et al 2011) as below:…”

Section: Materialmentioning

confidence: 99%

“…the active sites of ACE were bound competitively by casein hydrolysate and the treated hydrolysates, showing a classic competitive inhibition pattern. Some studies indicated that ACE-inhibitory peptides from food proteins were competitive inhibitors to ACE, such as freshwater clam hydrolysate (Sun et al 2011), separated peptides from fermented oyster sauce (Je et al 2005) and chymotryptic hydrolysate of a-kafirin (Kamath et al 2007). The present result was consistent with these reported results.…”

Section: Ace-inhibition Kinetics Of the Treated Casein Hydrolysatesmentioning

confidence: 99%

Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

Zhang¹,

Zhao²

2013

Czech J. Food Sci.

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Zhang Y., Zhao X.-H. (2013): Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium. Czech J. Food Sci., 31: 559-567.Casein hydrolysate with in vitro ACE-inhibitory activity of 44.4% at 0.3 mg/ml was generated from casein by Alcalase and modified by the Alcalase-catalysed plastein reaction in an ethanol-water medium. Eight treated hydrolysates were prepared using the reaction time of 1-8 h under ethanol or substrate concentration, Alcalase addition and reaction temperature of 56.8% (v/v) or 56.8% (w/v), 8.4 kU/g peptides and 37.5°C, respectively. Most of the treated hydrolysates showed enhanced ACE-inhibition compared to casein hydrolysate, and a reaction time of 4 h brought about the highest ACE-inhibition. All treated hydrolysates had lower zinc-or calcium-chelation but slightly higher iron(II)-chelation than casein hydrolysate, and a reaction time of 4 or 2 h could grant the treated hydrolysates the highest zinc-or calcium-chelation. Kinetic evaluation indicated that casein hydrolysate and two treated hydrolysates were competitive inhibitors to ACE. ACE-inhibition of these evaluated hydrolysates originated from themselves but was uncorrelated with their zinc-chelation, while their CaCO 3 precipitation inhibition was clearly correlated with their measured calcium-chelation (P < 0.05).

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“…Normally, the bioactive peptide is composed of 3-20 amino acids, and the molecular weight is less than 6 kDa (Kim & Wijesekara 2010;Samadi & Ismail 2010). Many studies have shown that bioactive peptides have many functional properties, such as a lowering of blood pressure (Bougatef et al 2008;Sun et al 2011;Ko et al 2012a), as well as antioxidant (Rajapakse et al 2005a;Ko et al 2012b;Girgih et al 2013), anti-inflammatory (Yang et al 2012), and antibacterial properties (McCann et al 2006).…”

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confidence: 99%

Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis

Zhouyong¹,

Tian²,

Xu³

et al. 2017

Czech J. Food Sci.

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Dong Z., Tian G., Xu Z., Li M., Xu M., Zhou Y., Ren H. (2017): Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis. Czech J. Food Sci., 35: 328-338.The freshwater mussel protein was hydrolysed using ultrasound-assisted enzymolysis. Ultrasound-assisted freshwater mussel protein hydrolysates (UPH) were divided into four fractions (> 10, 6-10, 3-6, and < 3 kDa) using ultrafiltration, and the fraction with the highest antioxidant activity was further subdivided into four fractions (F 1 -F 4 ) using gel chromatography. The amino acid compositions and antioxidant activities (DPPH, hydroxyl and superoxide radical scavenging activities, reducing power, ferrous ion chelating activity, and inhibition of linoleic acid oxidation) of peptide fractions were investigated. The results showed that the antioxidant activity of the < 3 kDa fraction was significantly higher than that of UPH, > 10, 6-10, and 3-6 kDa fractions. The antioxidant activity of F 2 was again higher compared with the < 3 kDa fraction and higher than that of F 1 , F 3 , and F 4 . Amino acid analysis showed that the antioxidant activities (except for chelating activity) of peptides increased with increasing hydrophobic amino acid content. The < 3 kDa and F 2 fractions exhibited strong inhibition of linoleic acid oxidation, their effects being even better than that of ascorbic acid (Vc) and l-glutathione (GSH). Therefore, these peptide fractions from freshwater mussel may be a potential natural antioxidant that could be added to various foods.

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Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of hydrolysates generated from byproducts of freshwater clam

Cited by 12 publications

References 23 publications

Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

Hydrolysis of Nyamplung (Calophylluminophyllum) protein and their antioxidant activity

Properties of casein hydrolysate as affected by plastein reaction in ethanol-water medium

Antioxidant activities of peptide fractions derived from freshwater mussel protein using ultrasound-assisted enzymatic hydrolysis

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