Isolation, purification and characterisation of angiotensin I-converting enzyme-inhibitory peptides derived from catfish (Clarias batrachus) muscle protein thermolysin hydrolysates

Masomeh Ghassem, Keizo Arihara, Abd. Salam Babji

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

The angiotensin I-converting enzyme (ACE)-inhibitory activities of catfish (Clarias batrachus) muscle protein hydrolysates were investigated. Thermolytic digests of C. batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration, gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC). The amino acid sequences of hydrolysates with the highest ACE-inhibitory activities were determined using electrospray quadrupole time-of-flight tandem mass spectrometry (ESI-TOFQ MS/MS). The sequences of GPPP (IC 50 = 0.86 μm) and IEKPP (IC 50 = 1.2 μm) corresponding to the fragments 986-989 and 441-445 of myosin-I heavy chain were identified for the sarcoplasmic and myofibrillar protein hydrolysates, respectively. Peptide GPPP exhibited a mixed-type inhibition whereas peptide IEKPP could only bind to the active sites of ACE. The results demonstrate that hydrolysates of C. batrachus muscle proteins obtained by thermolysin may contain bioactive peptides.

Original languageEnglish
Pages (from-to)2444-2451
Number of pages8
JournalInternational Journal of Food Science and Technology
Volume47
Issue number11
DOIs
Publication statusPublished - Nov 2012

Fingerprint

Thermolysin
Clarias batrachus
Protein Hydrolysates
Catfishes
Muscle Proteins
protein hydrolysates
peptidyl-dipeptidase A
muscle protein
Peptidyl-Dipeptidase A
catfish
Peptides
Purification
Muscle
Enzymes
peptides
Proteins
myofibrillar proteins
Enzyme activity
hydrolysates
inhibitory concentration 50

Keywords

  • Angiotensin I-converting enzyme-inhibitory activity
  • Bioactive peptides
  • Clarias batrachus
  • Tandem mass spectrometry
  • Thermolytic digest

ASJC Scopus subject areas

  • Food Science
  • Industrial and Manufacturing Engineering

Cite this

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title = "Isolation, purification and characterisation of angiotensin I-converting enzyme-inhibitory peptides derived from catfish (Clarias batrachus) muscle protein thermolysin hydrolysates",
abstract = "The angiotensin I-converting enzyme (ACE)-inhibitory activities of catfish (Clarias batrachus) muscle protein hydrolysates were investigated. Thermolytic digests of C. batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration, gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC). The amino acid sequences of hydrolysates with the highest ACE-inhibitory activities were determined using electrospray quadrupole time-of-flight tandem mass spectrometry (ESI-TOFQ MS/MS). The sequences of GPPP (IC 50 = 0.86 μm) and IEKPP (IC 50 = 1.2 μm) corresponding to the fragments 986-989 and 441-445 of myosin-I heavy chain were identified for the sarcoplasmic and myofibrillar protein hydrolysates, respectively. Peptide GPPP exhibited a mixed-type inhibition whereas peptide IEKPP could only bind to the active sites of ACE. The results demonstrate that hydrolysates of C. batrachus muscle proteins obtained by thermolysin may contain bioactive peptides.",
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N2 - The angiotensin I-converting enzyme (ACE)-inhibitory activities of catfish (Clarias batrachus) muscle protein hydrolysates were investigated. Thermolytic digests of C. batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration, gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC). The amino acid sequences of hydrolysates with the highest ACE-inhibitory activities were determined using electrospray quadrupole time-of-flight tandem mass spectrometry (ESI-TOFQ MS/MS). The sequences of GPPP (IC 50 = 0.86 μm) and IEKPP (IC 50 = 1.2 μm) corresponding to the fragments 986-989 and 441-445 of myosin-I heavy chain were identified for the sarcoplasmic and myofibrillar protein hydrolysates, respectively. Peptide GPPP exhibited a mixed-type inhibition whereas peptide IEKPP could only bind to the active sites of ACE. The results demonstrate that hydrolysates of C. batrachus muscle proteins obtained by thermolysin may contain bioactive peptides.

AB - The angiotensin I-converting enzyme (ACE)-inhibitory activities of catfish (Clarias batrachus) muscle protein hydrolysates were investigated. Thermolytic digests of C. batrachus sarcoplasmic and myofibrillar proteins exhibited inhibitory activity towards ACE and were purified with the aim of ultrafiltration, gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC). The amino acid sequences of hydrolysates with the highest ACE-inhibitory activities were determined using electrospray quadrupole time-of-flight tandem mass spectrometry (ESI-TOFQ MS/MS). The sequences of GPPP (IC 50 = 0.86 μm) and IEKPP (IC 50 = 1.2 μm) corresponding to the fragments 986-989 and 441-445 of myosin-I heavy chain were identified for the sarcoplasmic and myofibrillar protein hydrolysates, respectively. Peptide GPPP exhibited a mixed-type inhibition whereas peptide IEKPP could only bind to the active sites of ACE. The results demonstrate that hydrolysates of C. batrachus muscle proteins obtained by thermolysin may contain bioactive peptides.

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