In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate

There is no study on food-derived peptide with both anticoagulant and angiotensin I-converting enzyme inhibitory (ACEI) activities yet. In this work, the anticoagulant and ACEI activities of the casein hydrolysates released by pepsin digestion were evaluated for the first time to the best of our kno...

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Main Authors: Maolin Tu, Xinyu Qiao, Cong Wang, Hanxiong Liu, Shuzhen Cheng, Zhe Xu, Ming Du
Format: Article
Language:English
Published: Tsinghua University Press 2021-01-01
Series:Food Science and Human Wellness
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Online Access:http://www.sciencedirect.com/science/article/pii/S2213453020302007
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author Maolin Tu
Xinyu Qiao
Cong Wang
Hanxiong Liu
Shuzhen Cheng
Zhe Xu
Ming Du
author_facet Maolin Tu
Xinyu Qiao
Cong Wang
Hanxiong Liu
Shuzhen Cheng
Zhe Xu
Ming Du
author_sort Maolin Tu
collection DOAJ
description There is no study on food-derived peptide with both anticoagulant and angiotensin I-converting enzyme inhibitory (ACEI) activities yet. In this work, the anticoagulant and ACEI activities of the casein hydrolysates released by pepsin digestion were evaluated for the first time to the best of our knowledge. Results indicated that the casein hydrolysate exhibited potent anticoagulant activity by prolonging the thrombin time (TT) and the activated partial thromboplastin time (APTT). Compared with control samples, at 10 mg/mL, the TT and APTT of casein hydrolysate were 186.0 % ± 6.6 % and 163.5 % ± 7.4 %, respectively. The casein hydrolysate also showed a strong ACEI activity with an IC50 value of 1.775 mg/mL. The components of the bioactive casein hydrolysate were analyzed by nanoscale liquid chromatography quadrupole time-of-flight tandem mass spectrometry (NanoLC-Q-TOF-MS/MS). Total of 115 peptides were identified, among which 34, 9, 55 and 17 peptides were derived from αs1-, αs2-, β-, and κ-casein, respectively. The results of PeptideRanker and PepSite 2 analysis showed that 6 peptides (FRQFYQL, NENLLRF, NPWDQVKR, PVVVPPFLQ, PVRGPFPIIV, and ARHPHPHLSF) have both ACEI and anticoagulant activities by binding to the active sites of ACE and thrombin. This study indicated that casein is a potential functional food supplement that can be used for medical purposes.
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spelling doaj-art-7d8ede8ac24e4f1fb8b49da0651705be2025-02-03T05:18:51ZengTsinghua University PressFood Science and Human Wellness2213-45302021-01-011013237In vitro and in silico analysis of dual-function peptides derived from casein hydrolysateMaolin Tu0Xinyu Qiao1Cong Wang2Hanxiong Liu3Shuzhen Cheng4Zhe Xu5Ming Du6School of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaSchool of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaCorresponding author.; School of Food Science and Technology, National Engineering Research Center of Seafood, Collaborative Innovation Center of Seafood Deep Processing, Dalian Polytechnic University, Dalian 116034, ChinaThere is no study on food-derived peptide with both anticoagulant and angiotensin I-converting enzyme inhibitory (ACEI) activities yet. In this work, the anticoagulant and ACEI activities of the casein hydrolysates released by pepsin digestion were evaluated for the first time to the best of our knowledge. Results indicated that the casein hydrolysate exhibited potent anticoagulant activity by prolonging the thrombin time (TT) and the activated partial thromboplastin time (APTT). Compared with control samples, at 10 mg/mL, the TT and APTT of casein hydrolysate were 186.0 % ± 6.6 % and 163.5 % ± 7.4 %, respectively. The casein hydrolysate also showed a strong ACEI activity with an IC50 value of 1.775 mg/mL. The components of the bioactive casein hydrolysate were analyzed by nanoscale liquid chromatography quadrupole time-of-flight tandem mass spectrometry (NanoLC-Q-TOF-MS/MS). Total of 115 peptides were identified, among which 34, 9, 55 and 17 peptides were derived from αs1-, αs2-, β-, and κ-casein, respectively. The results of PeptideRanker and PepSite 2 analysis showed that 6 peptides (FRQFYQL, NENLLRF, NPWDQVKR, PVVVPPFLQ, PVRGPFPIIV, and ARHPHPHLSF) have both ACEI and anticoagulant activities by binding to the active sites of ACE and thrombin. This study indicated that casein is a potential functional food supplement that can be used for medical purposes.http://www.sciencedirect.com/science/article/pii/S2213453020302007CaseinAnticoagulantACE inhibitoryDual-functionNanoLC-Q-TOF-MS/MS
spellingShingle Maolin Tu
Xinyu Qiao
Cong Wang
Hanxiong Liu
Shuzhen Cheng
Zhe Xu
Ming Du
In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
Food Science and Human Wellness
Casein
Anticoagulant
ACE inhibitory
Dual-function
NanoLC-Q-TOF-MS/MS
title In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
title_full In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
title_fullStr In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
title_full_unstemmed In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
title_short In vitro and in silico analysis of dual-function peptides derived from casein hydrolysate
title_sort in vitro and in silico analysis of dual function peptides derived from casein hydrolysate
topic Casein
Anticoagulant
ACE inhibitory
Dual-function
NanoLC-Q-TOF-MS/MS
url http://www.sciencedirect.com/science/article/pii/S2213453020302007
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