Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysates of Tilapia (Oreochromis niloticus) Frame Protein

Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant ac...

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Published inMolecules (Basel, Switzerland) Vol. 17; no. 11; pp. 12836 - 12850
Main Authors Fan, Jian, He, Jintang, Zhuang, Yongliang, Sun, Liping
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 01.11.2012
MDPI
Subjects
Amino Acid Sequence
Animals
antioxidant peptide
Antioxidants
Biphenyl Compounds - chemistry
Chromatography
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Chromatography, Reverse-Phase
Cichlids
enzymatic hydrolysis
Fish Proteins - chemistry
Fish Proteins - isolation & purification
Free Radical Scavengers - chemistry
Free Radical Scavengers - isolation & purification
Free radicals
Free Radicals - chemistry
Hydrogen Peroxide - chemistry
Hydrolysis
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
Peptide Hydrolases - chemistry
Peptides
Picrates - chemistry
Proteins
Proteolysis
purification
Skin
Superoxides - chemistry
Tilapia
tilapia frame protein
Ultrafiltration
Online AccessGet full text

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Abstract Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC50 values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (•O2), hydrogen peroxides (H2O2) and hydroxyl radical (•OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC50 values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
AbstractList Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC(50) values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (*O(2)), hydrogen peroxides (H(2)O(2)) and hydroxyl radical (*OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC(50) values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC 50 values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical ( • O 2 ), hydrogen peroxides (H 2 O 2 ) and hydroxyl radical (•OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC 50 values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC50 values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (•O2), hydrogen peroxides (H2O2) and hydroxyl radical (•OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC50 values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC(50) values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (*O(2)), hydrogen peroxides (H(2)O(2)) and hydroxyl radical (*OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC(50) values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC(50) values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (*O(2)), hydrogen peroxides (H(2)O(2)) and hydroxyl radical (*OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC(50) values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain antioxidant peptides. The tilapia frame protein hydrolysate (TFPH) obtained by trypsin exhibited the highest degree of hydrolysis and antioxidant activity. Three series of peptides (TFPH1, TFPH 2 and TFPH 3) were obtained by ultrafiltration of TFPH through molecular weight cut-off membranes of 5, 3 and 1 kDa, respectively, and their IC50 values on scavenging 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical, superoxide anion radical (•O2), hydrogen peroxides (H2O2) and hydroxyl radical (•OH) activities were determined and compared with glutathione (GSH). The results showed that TFPH1 had the highest antioxidant activity. TFPH1 was further purified using ion exchange chromatography, gel filtration chromatography, and reversed phase high performance liquid chromatography (RP-HPLC). Finally, two antioxidant peptides were identified and the amino acid sequences were identified as Asp-Cys-Gly-Tyr (456.12 Da) and Asn-Tyr-Asp-Glu-Tyr (702.26 Da), respectively. The IC50 values of two peptides on hydroxyl radical scavenging activity were 27.6 and 38.4 μg/mL, respectively.
Author Zhuang, Yongliang
Fan, Jian
Sun, Liping
He, Jintang
AuthorAffiliation College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming 650500, China; Email: fj_3332000@yahoo.com.cn (J.F.); kmustslp@hotmail.com (J.H.); kmylzhuang@yahoo.com.cn (Y.Z.)
AuthorAffiliation_xml – name: College of Chemistry and Engineering, Kunming University of Science and Technology, Kunming 650500, China; Email: fj_3332000@yahoo.com.cn (J.F.); kmustslp@hotmail.com (J.H.); kmylzhuang@yahoo.com.cn (Y.Z.)
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  surname: Zhuang
  fullname: Zhuang, Yongliang
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  surname: Sun
  fullname: Sun, Liping
BackLink https://www.ncbi.nlm.nih.gov/pubmed/23117426$$D View this record in MEDLINE/PubMed
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Snippet Tilapia frame protein was hydrolyzed by different proteases, including properase E, pepsin, trypsin, flavourzyme, neutrase, gc106 and papain, to obtain...
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StartPage 12836
SubjectTerms Amino Acid Sequence
Animals
antioxidant peptide
Antioxidants
Biphenyl Compounds - chemistry
Chromatography
Chromatography, Gel
Chromatography, High Pressure Liquid
Chromatography, Ion Exchange
Chromatography, Reverse-Phase
Cichlids
enzymatic hydrolysis
Fish Proteins - chemistry
Fish Proteins - isolation & purification
Free Radical Scavengers - chemistry
Free Radical Scavengers - isolation & purification
Free radicals
Free Radicals - chemistry
Hydrogen Peroxide - chemistry
Hydrolysis
Peptide Fragments - chemistry
Peptide Fragments - isolation & purification
Peptide Hydrolases - chemistry
Peptides
Picrates - chemistry
Proteins
Proteolysis
purification
Skin
Superoxides - chemistry
Tilapia
tilapia frame protein
Ultrafiltration
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Title Purification and Identification of Antioxidant Peptides from Enzymatic Hydrolysates of Tilapia (Oreochromis niloticus) Frame Protein
URI https://www.ncbi.nlm.nih.gov/pubmed/23117426
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