Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers.
Enzyme hydrolysates (trypsin, papain, pepsin, α-chymotrypsin, and pepsin-pancreatin) of Tinospora cordifolia stem proteins were analyzed for antioxidant efficacy by measuring (1) 1,1-diphenyl-2-picrylhydrazyl (DPPH•) radical scavenging activity, (2) 2,20-azinobis(3-ethylbenzothiazoline-6-sulfonic ac...
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doaj-ff5cacdc696844c6859c0181be3611522020-11-24T21:35:15ZengPublic Library of Science (PLoS)PLoS ONE1932-62032018-01-01133e019371710.1371/journal.pone.0193717Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers.Raman PachaiappanEkant TamboliAurovind AcharyaChia-Hung SuSubash C B GopinathYeng ChenPalaniyandi VelusamyEnzyme hydrolysates (trypsin, papain, pepsin, α-chymotrypsin, and pepsin-pancreatin) of Tinospora cordifolia stem proteins were analyzed for antioxidant efficacy by measuring (1) 1,1-diphenyl-2-picrylhydrazyl (DPPH•) radical scavenging activity, (2) 2,20-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS+) radical scavenging capacity, and (3) Fe2+ chelation. Trypsin hydrolysate showed the strongest DPPH• scavenging, while α-chymotrypsin hydrolysate exhibited the highest ABTS+ scavenging and Fe2+ chelation. Undigested protein strongly inhibited the gastrointestinal enzymes, trypsin (50% inhibition at enzyme/substrate ratio = 1:6.9) and α-chymotrypsin (50% inhibition at enzyme/substrate ratio = 1:1.82), indicating the prolonged antioxidant effect after ingestion. Furthermore, gel filtration purified peptide fractions of papain hydrolysates exhibited a significantly higher ABTS+ and superoxide radical scavenging as compared to non-purified digests. Active fraction 9 showing the highest radical scavenging ability was further purified and confirmed by MALDI-TOF MS followed by MS/MS with probable dominant peptide sequences identified are VLYSTPVKMWEPGR, VITVVATAGSETMR, and HIGININSR. The obtained results revealed that free radical scavenging capacity of papain hydrolysates might be related to its consistently low molecular weight hydrophobic peptides.http://europepmc.org/articles/PMC5832316?pdf=render |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Raman Pachaiappan Ekant Tamboli Aurovind Acharya Chia-Hung Su Subash C B Gopinath Yeng Chen Palaniyandi Velusamy |
spellingShingle |
Raman Pachaiappan Ekant Tamboli Aurovind Acharya Chia-Hung Su Subash C B Gopinath Yeng Chen Palaniyandi Velusamy Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. PLoS ONE |
author_facet |
Raman Pachaiappan Ekant Tamboli Aurovind Acharya Chia-Hung Su Subash C B Gopinath Yeng Chen Palaniyandi Velusamy |
author_sort |
Raman Pachaiappan |
title |
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. |
title_short |
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. |
title_full |
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. |
title_fullStr |
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. |
title_full_unstemmed |
Separation and identification of bioactive peptides from stem of Tinospora cordifolia (Willd.) Miers. |
title_sort |
separation and identification of bioactive peptides from stem of tinospora cordifolia (willd.) miers. |
publisher |
Public Library of Science (PLoS) |
series |
PLoS ONE |
issn |
1932-6203 |
publishDate |
2018-01-01 |
description |
Enzyme hydrolysates (trypsin, papain, pepsin, α-chymotrypsin, and pepsin-pancreatin) of Tinospora cordifolia stem proteins were analyzed for antioxidant efficacy by measuring (1) 1,1-diphenyl-2-picrylhydrazyl (DPPH•) radical scavenging activity, (2) 2,20-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS+) radical scavenging capacity, and (3) Fe2+ chelation. Trypsin hydrolysate showed the strongest DPPH• scavenging, while α-chymotrypsin hydrolysate exhibited the highest ABTS+ scavenging and Fe2+ chelation. Undigested protein strongly inhibited the gastrointestinal enzymes, trypsin (50% inhibition at enzyme/substrate ratio = 1:6.9) and α-chymotrypsin (50% inhibition at enzyme/substrate ratio = 1:1.82), indicating the prolonged antioxidant effect after ingestion. Furthermore, gel filtration purified peptide fractions of papain hydrolysates exhibited a significantly higher ABTS+ and superoxide radical scavenging as compared to non-purified digests. Active fraction 9 showing the highest radical scavenging ability was further purified and confirmed by MALDI-TOF MS followed by MS/MS with probable dominant peptide sequences identified are VLYSTPVKMWEPGR, VITVVATAGSETMR, and HIGININSR. The obtained results revealed that free radical scavenging capacity of papain hydrolysates might be related to its consistently low molecular weight hydrophobic peptides. |
url |
http://europepmc.org/articles/PMC5832316?pdf=render |
work_keys_str_mv |
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