<i>In vitro</i>angiotensin-converting enzyme inhibition or digestive stability of casein hydrolysates treated by plastein reaction in propanol–water medium

Zhao, Bo; Zhao, Xin‐Huai

doi:10.1080/19476337.2012.748693

Cited by 3 publications

(4 citation statements)

References 33 publications

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“…Journal Pre-proof 48.2% [504]. When this product was modified by plastein reaction in propanol-water medium with addition of tyrosine or phenylalanine, after 1 h of reaction, produced modified hydrolysates with an inhibitory activity of 61.6-68.5% [504].…”

Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Use of Alcalase in the production of bioactive peptides: A review

Tacias-Pascacio

Morellon‐Sterling

Siar

et al. 2020

International Journal of Biological Macromolecules

224

114

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Section: J O U R N a L P R E -P R O O Fmentioning

confidence: 99%

Use of Alcalase in the production of bioactive peptides: A review

Tacias-Pascacio

Morellon‐Sterling

Siar

et al. 2020

International Journal of Biological Macromolecules

224

114

View full text Add to dashboard Cite

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“…The plastein reaction, which involves condensation and transpeptidation and contributes to peptide chain growth and synthesis (Yamashita et al 1971), can be used to improve the nutritional value of proteins that are limiting in essential amino acids (SPH, methionine, cysteine and lysine) or reduce the content of other amino acids (SPH, phenylalanine) for dietetic applications (Yamashita et al 1976). The plastein reaction in water or other media enhanced the in vitro inhibition of angiotensin I converting enzyme, the antioxidant activity of protein hydrolysates (Zhao et al 2010;Sun and Zhao 2012;Yue et al 2013;Zhao and Zhao 2013) and the cytoprotection of casein hydrolysates on rat hepatocytes (Zhao et al 2014). The plastein reaction of casein hydrolysates in ethanol-water showed an impact on the mineral-chelating activity (including of calcium, zinc and iron) and inhibition of the calcium carbonate precipitation (Zhang and Zhao 2013).…”

Section: Introductionmentioning

confidence: 97%

“…; Sun and Zhao ; Yue et al . ; Zhao and Zhao ) and the cytoprotection of casein hydrolysates on rat hepatocytes (Zhao et al . ).…”

Section: Introductionmentioning

confidence: 99%

In VitroCalcium-Chelating and Platelet Anti-Aggregation Activities of Soy Protein Hydrolysate Modified by the Alcalase-Catalyzed Plastein Reaction

Zhang

Zhao

2014

Journal of Food Biochemistry

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Soy protein hydrolysate (SPH) (1 mg/mL), generated by alcalase, had a calcium‐chelating activity of 41 mg/g peptide. The alcalase‐catalyzed plastein reaction of SPH was carried out in different media: ethanol–water, methanol–water and water. The effects of SPH and of resulting modified hydrolysates on calcium‐chelating activities and inhibition of calcium precipitation and platelet aggregation were assessed in vitro. The optimum ethanol concentration, alcalase level and reaction temperature for the plastein reaction was 56.8% v/v, 5.26 kU/g peptide and 33.1C, respectively. The modified hydrolysates had better calcium‐chelating activities and stronger inhibition of calcium precipitation and platelet aggregation than SPH. The modified hydrolysate with the highest calcium‐chelating activity showed the strongest inhibitory effects on platelet aggregation and calcium precipitation. The plastein reaction enhances the in vitro calcium‐chelating and platelet anti‐aggregation activities of SPH. Practical Applications In this study, an alcalase‐catalyzed plastein reaction carried out in three media (ethanol–water, methanol–water and water) was used to modify the in vitro calcium‐chelating and platelet anti‐aggregation activities of an alcalase‐generated soy protein hydrolysate. The results revealed that the modified hydrolysates of higher calcium‐chelating activity had stronger inhibitory effects on platelet aggregation and calcium precipitation. The results of this study provide further insight on the enzymatic synthesis of bioactive peptides of higher activity using the plastein reaction.

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“…ACE-inhibitory activity was measured by a spectrophotometric method used by Zhao and Zhao (2013). Lineweaver-Burk plots were applied to measure Michaelis-Menten equation and inhibition kinetics (Barbana & Boye 2011).…”

Section: Materialmentioning

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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In vitroangiotensin-converting enzyme inhibition or digestive stability of casein hydrolysates treated by plastein reaction in propanol–water medium

Cited by 3 publications

References 33 publications

Use of Alcalase in the production of bioactive peptides: A review

Use of Alcalase in the production of bioactive peptides: A review

In VitroCalcium-Chelating and Platelet Anti-Aggregation Activities of Soy Protein Hydrolysate Modified by the Alcalase-Catalyzed Plastein Reaction

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

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